American Chemical Society
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. 31P 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.
O'Connor, Casey and Kovriguine, Evgueni, "Global Conformational Dynamics in Ras" (2008). Chemistry Faculty Research and Publications. 236.
ADA Accessible Version
Accepted version. Biochemistry, Vol. 47, No. 39 (September 2008): 10244-10246. DOI. © 2008 American Chemical Society. Used with permission.