The changing landscape of protein allostery

doi:10.1016/j.sbi.2006.01.003

Review

. 2006 Feb;16(1):102-8.

doi: 10.1016/j.sbi.2006.01.003. Epub 2006 Jan 19.

The changing landscape of protein allostery

Joanna F Swain¹, Lila M Gierasch

Affiliations

Affiliation

¹ Department of Biochemistry & Molecular Biology, Department of Chemistry, 710 North Pleasant Street, University of Massachusetts, Amherst, MA 01003-9305, USA.

PMID: 16423525
DOI: 10.1016/j.sbi.2006.01.003

Review

The changing landscape of protein allostery

Joanna F Swain et al. Curr Opin Struct Biol. 2006 Feb.

. 2006 Feb;16(1):102-8.

doi: 10.1016/j.sbi.2006.01.003. Epub 2006 Jan 19.

Authors

Joanna F Swain¹, Lila M Gierasch

Affiliation

¹ Department of Biochemistry & Molecular Biology, Department of Chemistry, 710 North Pleasant Street, University of Massachusetts, Amherst, MA 01003-9305, USA.

PMID: 16423525
DOI: 10.1016/j.sbi.2006.01.003

Abstract

It is becoming increasingly clear that the fundamental capacity to undergo conformational change in response to ligand binding is intrinsic to proteins. This property confers on proteins the ability to be allosterically modulated in order to shift substrate binding affinities, alter enzymatic activity or regulate protein-protein interaction. How this allosteric modulation occurs--the pathways of communication, the shifting of conformational ensembles and the altered molecular dynamics--has received considerable attention during the past two years. Recent progress has helped outline the molecular origins of allostery in proteins as diverse as Hsp70 molecular chaperones and signal integrating proteins, such as WASP. In addition, allosteric properties have been successfully engineered into proteins for drug design or the development of novel biosensors. Methodological advances have provided exciting prospects for new insights and new biological roles of allosteric systems have been uncovered.

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The changing landscape of protein allostery

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The changing landscape of protein allostery

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