Global conformational dynamics in ras.
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.
O'Connor
Casey
C
Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, Wisconsin 53226, USA.
Kovrigin
Evgenii L
EL
D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D018631:ras Proteins / Q000737:chemistry* / Q000378:metabolism
D006160:Guanosine Triphosphate; D018631:ras Proteins