Source 1primary paper2011Journal of Biological Chemistry
Toolkit/integrin αIIb cytoplasmic domain
integrin αIIb cytoplasmic domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The integrin αIIb cytoplasmic domain is a platelet integrin tail segment that functions as a specific binding partner for the calcium- and integrin-binding protein CIB1. Solution structural analysis indicates that this interaction involves EF-hand III of CIB1 and is associated with a CIB1 conformational response distinct from that of related EF-hand proteins.
Usefulness & Problems
Why this is useful
This domain is useful as a defined peptide-binding element for studying and exploiting the specific CIB1–αIIb interaction. It provides a biologically grounded handle for probing CIB1 recognition by an integrin cytoplasmic tail in the context of Ca2+-CIB1 and Mg2+-CIB1.
Problem solved
It helps address the problem of obtaining a specific protein interaction module for CIB1 rather than relying on less specific EF-hand protein interactions. The cited work specifically maps the CIB1-contacting region to EF-hand III, clarifying the molecular interface used for αIIb tail recognition.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
binding-induced conformational changebinding-induced conformational changeHeterodimerizationHeterodimerizationHeterodimerizationTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: actuatoroperating role: sensorswitch architecture: multi componentswitch architecture: recruitment
Practical use is currently defined mainly by its interaction with CIB1, including both Ca2+-bound and Mg2+-bound CIB1 states examined in solution structural work. The supplied evidence does not specify construct boundaries, expression format, delivery strategy, or whether the isolated αIIb cytoplasmic domain is sufficient in all experimental contexts.
The evidence provided is limited to a single 2011 study centered on structural characterization of the CIB1 side of the interaction. The supplied evidence does not report quantitative affinity, transferability to engineered systems, or validation in applications beyond the native binding context.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
CIB1 behaves differently from related EF-hand regulatory calcium-binding proteins such as calmodulin or neuronal calcium sensor proteins.
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
CIB1 behaves differently from related EF-hand regulatory calcium-binding proteins such as calmodulin or neuronal calcium sensor proteins.
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
CIB1 behaves differently from related EF-hand regulatory calcium-binding proteins such as calmodulin or neuronal calcium sensor proteins.
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
CIB1 behaves differently from related EF-hand regulatory calcium-binding proteins such as calmodulin or neuronal calcium sensor proteins.
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
CIB1 behaves differently from related EF-hand regulatory calcium-binding proteins such as calmodulin or neuronal calcium sensor proteins.
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1.
Ca(2+)-CIB1 and Mg(2+)-CIB1 have similar structures, but the N-lobe of Mg(2+)-CIB1 is slightly more opened than that of Ca(2+)-CIB1.
Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1.
Ca(2+)-CIB1 and Mg(2+)-CIB1 have similar structures, but the N-lobe of Mg(2+)-CIB1 is slightly more opened than that of Ca(2+)-CIB1.
Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1.
Ca(2+)-CIB1 and Mg(2+)-CIB1 have similar structures, but the N-lobe of Mg(2+)-CIB1 is slightly more opened than that of Ca(2+)-CIB1.
Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1.
Ca(2+)-CIB1 and Mg(2+)-CIB1 have similar structures, but the N-lobe of Mg(2+)-CIB1 is slightly more opened than that of Ca(2+)-CIB1.
Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1.
Ca(2+)-CIB1 and Mg(2+)-CIB1 have similar structures, but the N-lobe of Mg(2+)-CIB1 is slightly more opened than that of Ca(2+)-CIB1.
The solution structure of Ca2+-CIB1 has smaller opened EF-hands in its C-domain than available crystal structures.
The solution structure of Ca(2+)-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures.
The solution structure of Ca2+-CIB1 has smaller opened EF-hands in its C-domain than available crystal structures.
The solution structure of Ca(2+)-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures.
The solution structure of Ca2+-CIB1 has smaller opened EF-hands in its C-domain than available crystal structures.
The solution structure of Ca(2+)-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures.
The solution structure of Ca2+-CIB1 has smaller opened EF-hands in its C-domain than available crystal structures.
The solution structure of Ca(2+)-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures.
The solution structure of Ca2+-CIB1 has smaller opened EF-hands in its C-domain than available crystal structures.
The solution structure of Ca(2+)-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug integrin-iib-cytoplasmic-domain
a specific binding partner for the platelet integrin αIIb cytoplasmic domain
Source:
binding interactionsupports
CIB1 is a specific binding partner for the platelet integrin αIIb cytoplasmic domain.
The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca(2+)-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain
Source:
binding site mappingsupports
EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 is directly involved in the interaction of CIB1 with αIIb.
The EF-hand III of both Ca(2+)-CIB1 and Mg(2+)-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb.
Source:
conformational changesupports
The C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding.
NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca(2+)-CIB1 is displaced upon αIIb binding.
Source:
Comparisons
Source-backed strengths
The interaction is supported by solution structural studies reported for both Ca2+-CIB1 and Mg2+-CIB1, which strengthens evidence that the αIIb cytoplasmic domain is a bona fide CIB1-binding partner. Binding-site mapping further localizes the interaction to EF-hand III of CIB1, providing mechanistic specificity.
Source:
Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
Compared with Arabidopsis thaliana cryptochrome 2
integrin αIIb cytoplasmic domain and Arabidopsis thaliana cryptochrome 2 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Relative tradeoffs: appears more independently replicated.
Compared with Q-PAS1
integrin αIIb cytoplasmic domain and Q-PAS1 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Compared with Rel/NF-κB family of transcription factors
integrin αIIb cytoplasmic domain and Rel/NF-κB family of transcription factors address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.