Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling.
The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf-RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular beta-sheet observed for the complex between Ras and Raf-RBD.
Geyer
M
M
Herrmann
C
C
Wohlgemuth
S
S
Wittinghofer
A
A
Kalbitzer
H R
HR
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019204:GTP-Binding Proteins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015398:Signal Transduction / Q000502:physiology*; D020668:rap GTP-Binding Proteins; D018631:ras Proteins / Q000737:chemistry*
D019204:GTP-Binding Proteins; D020668:rap GTP-Binding Proteins; D018631:ras Proteins