Work

Allostery and cooperativity revisited

Year: 2008

Type: review

Abstract: Although phenomenlogical models that account for cooperativity in allosteric systems date back to the early and mid-60's (e.g., the KNF and MWC models), there is resurgent interest in the topic due to the recent experimental and computational studies that attempted to reveal, at an atomistic level, how allostery actually works. In this review, using systems for which atomistic simulations have been carried out in our groups as examples, we describe the current understanding of allostery, how the mechanisms go beyond the classical MWC/Pauling-KNF descriptions, and point out that the "new view" of allostery, emphasizing "population shifts," is, in fact, an "old view." The presentation offers not only an up-to-date description of allostery from a theoretical/computational perspective, but also helps to resolve several outstanding issues concerning allostery.

Source: Protein Science

DOI: 10.1110/ps.03259908

Authors: Qiang Cui, Martin Karplus

Institutions: University of Wisconsin–Madison, Harvard University, Institut de Science et d'Ingénierie Supramoléculaires

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Harvard University, National Institutes of Health, National Institute of General Medical Sciences

Awards: Conformational Change in Molecular Biology, Coupling between conformation and chemistry in enzymes, G4922044601