Global Conformational Dynamics in Ras
Author(s) -
Casey M. O’Connor,
Evgenii L. Kovrigin
Publication year - 2008
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/bi801076c
Subject(s) - allosteric regulation , gtpase , gtp' , biophysics , protein dynamics , chemistry , conformational change , microbiology and biotechnology , molecular dynamics , gtp binding protein regulators , signaling proteins , dynamics (music) , function (biology) , signal transduction , protein structure , g protein , biochemistry , biology , enzyme , physics , computational chemistry , acoustics
Ras and its homologues are central to regulation of a multitude of cellular processes. Ras in complex with GTP binds and activates its downstream signaling partners. (31)P NMR studies indicated that the Ras-GTP conformation is heterogeneous on a millisecond time scale, but details of its conformational dynamics remain unknown. Here we present evidence that the conformational exchange process in human H-Ras complexed with GTP mimic GppNHp is global, encompassing most of the GTPase catalytic domain. The correlated character of conformational dynamics in Ras opens opportunities for understanding allosteric effects in Ras function.
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