Allosteric inhibition through suppression of transient conformational states.

doi:10.1038/nchembio.1250

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Article

Allosteric inhibition through suppression of transient conformational states.

Nature chemical biology - 1 Jul 2013

Tzeng Shiou-Ru, Kalodimos Charalampos G

Abstract excerpt

The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers several advantages over competitive inhibition, but the mechanisms of action remain poorly understood in most cases. Here we show that allosteric inhibition can be effected by destabilizing a low-populated conformational state that serves as an on-pathway...

Topics

Allosteric Site
Calorimetry
Cyclic AMP Receptor Protein
DNA
Escherichia coli
Ligands
Magnetic Resonance Spectroscopy
Models, Molecular
Mutation
Protein Binding
Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 23644478
DOI: 10.1038/nchembio.1250

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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