Source 1primary paper2013Biochemistry
Toolkit/α-integrin cytoplasmic tails
α-integrin cytoplasmic tails
Also known as: α-integrin CTs
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
α-integrin cytoplasmic tails are short intracellular integrin tail domains that bind calcium and integrin binding protein 1 (CIB1). Evidence indicates that multiple α-integrin cytoplasmic tails engage a shared hydrophobic pocket on CIB1 through a consensus binding site and can compete for CIB1 binding in vitro.
Usefulness & Problems
Why this is useful
These domains are useful as native protein interaction modules for probing CIB1 recognition of integrin tails and the structural basis of CIB1 binding promiscuity. The available evidence supports their use in studies of hydrophobic pocket-mediated binding and competition among α-integrin tail ligands.
Problem solved
They help address the problem of identifying how CIB1 recognizes multiple α-integrin cytoplasmic tails despite sequence variation. The cited work specifically links this recognition to a shared hydrophobic binding pocket and consensus-site-dependent interactions.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
competitive bindingconsensus motif-mediated recognitionprotein-protein binding via hydrophobic interactionsTechniques
Functional AssayTarget processes
recombinationInput: Thermal
Implementation Constraints
Practical use of these domains in the cited context depends on assaying interaction with CIB1, a calcium and integrin binding protein 1. The evidence supports construct designs that preserve the α-integrin cytoplasmic tail sequence features required for consensus-site and hydrophobic-pocket recognition, but it does not provide expression, delivery, or cofactor optimization details beyond the CIB1 identity.
The evidence is centered on CIB1 binding and in vitro competition, with no direct validation here for broader cellular functions or engineered applications. The supplied evidence also does not define which specific α-integrin tails were validated experimentally beyond reference to αIIb as a competitor benchmark.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2020UNC Libraries
Ranked Claims
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Approval Evidence
2 sources8 linked approval claimsfirst-pass slug integrin-cytoplasmic-tails
proteins that bind to α-integrin cytoplasmic tails (CTs)
Source:
α-integrin cytoplasmic tails (CTs)
Source:
binding mechanismsupports
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Source:
competitive bindingsupports
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Source:
computational binding predictionsupports
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Source:
sequence conservationsupports
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Source:
binding mechanismsupports
CIB1 binding to α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Source:
binding site conservationsupports
Key residues in the CIB1 binding site of αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site of αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Source:
competitive bindingsupports
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays, which showed that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Source:
computational binding predictionsupports
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Source:
Comparisons
Source-backed strengths
Structural, thermodynamic, and docking evidence all support a common CIB1-binding mode for multiple α-integrin cytoplasmic tails. In vitro competition data further indicate that distinct α-integrin tails can compete with the αIIb cytoplasmic tail for the same CIB1 interaction surface.
Ranked Citations
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