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Propagating conformational changes over long (and short) distances in proteins.

ABSTRACT: The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.

SUBMITTER: Yu EW

PROVIDER: S-EPMC55484 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature

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Propagating conformational changes over long (and short) distances in proteins.

Yu E W EW Koshland D E DE

Proceedings of the National Academy of Sciences of the United States of America 20010801 17

The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor tha ...[more]

PMID: 11504940

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