期刊
STRUCTURE
卷 18, 期 9, 页码 1094-1103出版社
CELL PRESS
DOI: 10.1016/j.str.2010.05.015
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资金
- Natural Sciences and Engineering Research Council of Canada
- National Science Foundation
- National Institute of Neurological Disorders and Stroke [R01NS056128]
- Canadian Institutes of Health Research
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-98CH10886]
Complete folding is not a prerequisite for protein function, as disordered and partially folded states of proteins frequently perform essential biological functions. In order to understand their functions at the molecular level, we utilized diverse experimental measurements to calculate ensemble models of three nonhomologous, intrinsically disordered proteins: 1-2, spinophilin, and DARPP-32, which bind to and regulate protein phosphatase 1 (PP1). The models demonstrate that these proteins have dissimilar propensities for secondary and tertiary structure in their unbound forms. Direct comparison of these ensemble models with recently determined PP1 complex structures suggests a significant role for transient, preformed structure in the interactions of these proteins with PP1. Finally, we generated an ensemble model of partially disordered 1-2 bound to PP1 that provides insight into the relationship between flexibility and biological function in this dynamic complex.
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