bioRxiv Biochemistry
bioRxiv Biochemistry
5 years ago

Effect of ligands on stability of H-Ras GTPase

Kovrigina, Kovrigin, O'Connor, E. A., E. L., C.
The G domain of a small monomeric GTPase Ras contains a nucleotide-binding pocket and a magnesium-binding site essential for the Ras function in cellular signaling. The G domain also has another (allosteric) ion-binding site on the rear surface of the G domain, which function is still unknown. In this paper, we detailed the effect of calcium and magnesium ions on stability of Ras bound to GDP, GTP, and GTP-mimic GppNHp. We revealed that the remote allosteric ion-binding site contributes very significantly to stability of Ras in the GDP-bound conformation, but nearly not at all - when Ras is bound to a GTP mimic. These findings highlight that further studies of the remote ion-binding site are warranted to reveal its role in the Ras function.

Publisher URL: http://biorxiv.org/cgi/content/short/179283v1

DOI: 10.1101/179283

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