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Dynamic equilibria in protein kinases.


ABSTRACT: Structural changes involved in protein kinase activation and ligand binding have been determined from a wealth of X-ray crystallographic evidence. Recent solution studies using NMR, EPR, HX-MS, and fluorescence techniques have deepened this understanding by highlighting the underlying energetics and dynamics of multistate conformational ensembles. This new research is showing how activation mechanisms and ligand binding alter the internal motions of kinases and enable allosteric coupling between distal regulatory regions and the active site.

SUBMITTER: Pegram LM 

PROVIDER: S-EPMC9718358 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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Dynamic equilibria in protein kinases.

Pegram Laurel M LM   Anderson Jake W JW   Ahn Natalie G NG  

Current opinion in structural biology 20210820


Structural changes involved in protein kinase activation and ligand binding have been determined from a wealth of X-ray crystallographic evidence. Recent solution studies using NMR, EPR, HX-MS, and fluorescence techniques have deepened this understanding by highlighting the underlying energetics and dynamics of multistate conformational ensembles. This new research is showing how activation mechanisms and ligand binding alter the internal motions of kinases and enable allosteric coupling between  ...[more]

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