Global Conformational Dynamics in Ras

Authors

Casey O'Connor, Medical College of Wisconsin
Evgueni Kovriguine, Marquette UniversityFollow

Document Type

Article

Publication Date

9-2008

Publisher

American Chemical Society

Source Publication

Biochemistry

Source ISSN

0006-2960

Abstract

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.

Comments

Accepted version. Biochemistry, Vol. 47, No. 39 (September 2008): 10244-10246. DOI. © 2008 American Chemical Society. Used with permission.

Recommended Citation

O'Connor, Casey and Kovriguine, Evgueni, "Global Conformational Dynamics in Ras" (2008). Chemistry Faculty Research and Publications. 236.
https://epublications.marquette.edu/chem_fac/236