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Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones
Author(s) -
He Lichun,
Hiller Sebastian
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900215
Subject(s) - chaperone (clinical) , protein folding , co chaperone , native state , complementarity (molecular biology) , computational biology , chemical chaperone , protein structure , biology , chemistry , biophysics , microbiology and biotechnology , biochemistry , genetics , unfolded protein response , heat shock protein , hsp90 , medicine , pathology , endoplasmic reticulum , gene
Molecular chaperones are crucial for cellular life to ensure that all proteins obtain their right fold and functionality. Many chaperones promiscuously bind a wide spectrum of client proteins, ranging from nascent to quasi‐native and native proteins. Several recent studies have investigated, at atomic resolution, how chaperones interact with native proteins. Native proteins feature a wide variety of structural conformations, and therefore, a given chaperone cannot accomplish full surface complementarity to all of its client proteins. This limitation is circumvented by the recognition of frustrated regions on the client protein surface by the chaperone. In this interaction mode, the chaperone forms a multitude of transient local interactions with some segments of the client, whereas other parts are transiently not in favorable interactions. A permanent rearrangement of the client conformation on the chaperone occurs. Reconfiguration on the chaperone surface also gives the client a chance to fold into its correct, minimally frustrated conformation.