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Science 21 September 1990:
Vol. 249. no. 4975, pp. 1425 - 1428
DOI: 10.1126/science.2402636
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Articles
Science, Vol 249, Issue 4975, 1425-1428
Copyright © 1990 by American Association for the Advancement of Science
Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop
D Joseph,
GA Petsko,
and
M Karplus
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Triosephosphate isomerase (TIM) is used as a model system for the study of how a localized conformational change in a protein structure is produced and related to enzyme reactivity. An 11-residue loop region moves more than 7 angstroms and closes over the active site when substrate binds. The loop acts like a "lid" in that it moves rigidly and is attached by two hinges to the remainder of the protein. The nature of the motion appears to be built into the loop by conserved residues; the hinge regions, in contrast, are not conserved. Results of molecular dynamics calculations confirm the structural analysis and suggest a possible ligand-induced mechanism for loop closure.
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