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Allosteric switch regulates protein-protein binding through collective motion.


ABSTRACT: Many biological processes depend on allosteric communication between different parts of a protein, but the role of internal protein motion in propagating signals through the structure remains largely unknown. Through an experimental and computational analysis of the ground state dynamics in ubiquitin, we identify a collective global motion that is specifically linked to a conformational switch distant from the binding interface. This allosteric coupling is also present in crystal structures and is found to facilitate multispecificity, particularly binding to the ubiquitin-specific protease (USP) family of deubiquitinases. The collective motion that enables this allosteric communication does not affect binding through localized changes but, instead, depends on expansion and contraction of the entire protein domain. The characterization of these collective motions represents a promising avenue for finding and manipulating allosteric networks.

SUBMITTER: Smith CA 

PROVIDER: S-EPMC4812760 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Allosteric switch regulates protein-protein binding through collective motion.

Smith Colin A CA   Ban David D   Pratihar Supriya S   Giller Karin K   Paulat Maria M   Becker Stefan S   Griesinger Christian C   Lee Donghan D   de Groot Bert L BL  

Proceedings of the National Academy of Sciences of the United States of America 20160309 12


Many biological processes depend on allosteric communication between different parts of a protein, but the role of internal protein motion in propagating signals through the structure remains largely unknown. Through an experimental and computational analysis of the ground state dynamics in ubiquitin, we identify a collective global motion that is specifically linked to a conformational switch distant from the binding interface. This allosteric coupling is also present in crystal structures and  ...[more]

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