Propagating conformational changes over long (and short) distances in proteins.
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.
Yu
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Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.
Koshland
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DE
D001059:Apoproteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D017459:Receptors, Amino Acid / Q000737:chemistry
D001059:Apoproteins; D001426:Bacterial Proteins; D017459:Receptors, Amino Acid; C031959:aspartic acid receptor