Literature DB >> 24740064

The ensemble nature of allostery.

Hesam N Motlagh1, James O Wrabl1, Jing Li1, Vincent J Hilser1.   

Abstract

Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.

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Year:  2014        PMID: 24740064      PMCID: PMC4224315          DOI: 10.1038/nature13001

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  106 in total

1.  Enzyme flexibility and enzyme action.

Authors:  D E KOSHLAND
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Review 2.  Atomic-level characterization of disordered protein ensembles.

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4.  The energy landscapes and motions of proteins.

Authors:  H Frauenfelder; S G Sligar; P G Wolynes
Journal:  Science       Date:  1991-12-13       Impact factor: 47.728

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Authors:  Ron O Dror; Robert M Dirks; J P Grossman; Huafeng Xu; David E Shaw
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Journal:  Proteins       Date:  2013-04-20

7.  Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms.

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Journal:  Proc Natl Acad Sci U S A       Date:  2006-05-22       Impact factor: 11.205

8.  The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor.

Authors:  Sean E Reichheld; Zhou Yu; Alan R Davidson
Journal:  Proc Natl Acad Sci U S A       Date:  2009-12-22       Impact factor: 11.205

9.  Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.

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10.  Exploring residue component contributions to dynamical network models of allostery.

Authors:  Adam T Vanwart; John Eargle; Zaida Luthey-Schulten; Rommie E Amaro
Journal:  J Chem Theory Comput       Date:  2012-07-05       Impact factor: 6.006

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  406 in total

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Authors:  Jingjing Guo; Huan-Xiang Zhou
Journal:  Chem Rev       Date:  2016-02-15       Impact factor: 60.622

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Authors:  Hesam N Motlagh; Jeremy A Anderson; Jing Li; Vincent J Hilser
Journal:  Biophys Rev       Date:  2015-04-23

8.  Structured States of Disordered Proteins from Genomic Sequences.

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10.  Structural basis for the catalytic mechanism and α-ketoglutarate cooperativity of glutamate dehydrogenase.

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