Source 1primary paper2023ACS Chemical Biology
Toolkit/catalytically inactive NS3 protease
catalytically inactive NS3 protease
Also known as: inactive NS3 protease
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Catalytically inactive NS3 protease is a protein domain repurposed as a high-affinity binder for genetically encoded antiviral peptides. In the reported system, peptide-bound NS3 complexes are displaced by FDA-approved NS3-targeting drugs to chemically control transcription, cell signaling, split-protein complementation, and allosteric Cre recombinase regulation.
Usefulness & Problems
Why this is useful
This tool enables chemical control of engineered protein functions through a drug-displaceable protein–peptide interaction rather than catalytic activity. It is useful for building regulatable systems that respond to clinically relevant NS3-targeting antivirals and for creating orthogonal recombination control in eukaryotic cells and across divergent organisms.
Source:
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Problem solved
It addresses the need for a genetically encoded, chemically actuated interaction module that can switch protein activities using small molecules. Specifically, it provides a new mechanism for allosteric regulation of Cre recombinase and supports control of transcription, signaling, and split-protein outputs through drug displacement.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
allosteric regulationallosteric regulationhigh-affinity peptide bindinghigh-affinity peptide bindingsmall-molecule drug displacementsmall-molecule drug displacementTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Chemical
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuatorswitch architecture: uncaging
Implementation is based on domain fusion using catalytically inactive NS3 protease together with genetically encoded antiviral peptides. Chemical input is provided by FDA-approved NS3-targeting drugs that displace the NS3–peptide complex; the evidence does not specify the exact NS3 variant, peptide sequence, or construct architecture.
The supplied evidence does not report quantitative binding, dynamic range, kinetics, or comparative performance against alternative chemically controlled interaction systems. Practical constraints such as drug-specific potency, background binding, construct size, and context dependence are not described in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
Approval Evidence
1 source1 linked approval claimfirst-pass slug catalytically-inactive-ns3-protease
utilizing catalytically inactive NS3 protease as a high affinity binder
Source:
toolkit expansionsupports
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
Source:
Comparisons
Source-backed strengths
The reported system uses catalytically inactive NS3 protease as a high-affinity binder and can be actuated by FDA-approved NS3-targeting drugs. Validation spans multiple functional outputs, including transcription, cell signaling, split-protein complementation, and allosteric Cre regulation, and the recombination control was reported to function in eukaryotic cells and in divergent organisms for control of prokaryotic recombinase activity.
Compared with basic helix-loop-helix (bHLH) domain
catalytically inactive NS3 protease and basic helix-loop-helix (bHLH) domain address a similar problem space.
Shared frame: same top-level item type; same primary input modality: chemical
Compared with CIB1
catalytically inactive NS3 protease and CIB1 address a similar problem space.
Shared frame: same top-level item type; same primary input modality: chemical
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with SMN tudor domain
catalytically inactive NS3 protease and SMN tudor domain address a similar problem space.
Shared frame: same top-level item type; same primary input modality: chemical
Ranked Citations
- 1.