NDLI: Exploring the origins of binding specificity through the computational redesign of calmodulin.

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Exploring the origins of binding specificity through the computational redesign of calmodulin.

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Exploring the origins of binding specificity through the computational redesign of calmodulin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shifman, Julia M. Mayo, Stephen L.
Description	Author Affiliation: Shifman JM ( Howard Hughes Medical Institute and Division of Biology, California Institute of Technology, Mail Code 114-96, Pasadena, CA 91125, USA.);
Abstract	Calmodulin (CaM) is a second messenger protein that has evolved to bind tightly to a variety of targets and, as such, exhibits low binding specificity. We redesigned CaM by using a computational protein design algorithm to improve its binding specificity for one of its targets, smooth muscle myosin light chain kinase (smMLCK). Residues in or near the CaM/smMLCK binding interface were optimized; CaM interactions with alternative targets were not directly considered in the optimization. The predicted CaM sequences were constructed and tested for binding to a set of eight targets including smMLCK. The best CaM variant, obtained from a calculation that emphasized intermolecular interactions, showed up to a 155-fold increase in binding specificity. The increase in binding specificity was not due to improved binding to smMLCK, but due to decreased binding to the alternative targets. This finding is consistent with the fact that the sequence of wild-type CaM is nearly optimal for interactions with numerous targets.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calmodulin Chemistry Algorithms Animals Computer Simulation Crystallography, X-Ray Dimerization Kinetics Models, Molecular Muscle, Smooth Metabolism Myosin-Light-Chain Kinase Peptides Protein Binding Protein Conformation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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