5UHV

wild-type NRas bound to GppNHp

5UHV の概要

• エントリーDOI: 10.2210/pdb5uhv/pdb
• 分子名称: GTPase NRas, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: nras, gtpase, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19435.82

構造登録者

Reid, D.,Johnson, C.,Salter, S.,Mattos, C. (登録日: 2017-01-12, 公開日: 2017-06-28, 最終更新日: 2023-10-04)

主引用文献

Johnson, C.W.,Reid, D.,Parker, J.A.,Salter, S.,Knihtila, R.,Kuzmic, P.,Mattos, C.
The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.
J. Biol. Chem., 292:12981-12993, 2017

PubMed Abstract: H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell proliferation, differentiation, and survival, and their mutants occur frequently in human cancers. The G-domain, which catalyzes GTP hydrolysis and mediates downstream signaling, is 95% conserved between the Ras isoforms. Because of their very high sequence identity, biochemical studies done on H-Ras have been considered representative of all three Ras proteins. We show here that this is not a valid assumption. Using enzyme kinetic assays under identical conditions, we observed clear differences between the three isoforms in intrinsic catalysis of GTP by Ras in the absence and presence of the Ras-binding domain (RBD) of the c-Raf kinase protein (Raf-RBD). Given their identical active sites, isoform G-domain differences must be allosteric in origin, due to remote isoform-specific residues that affect conformational states. We present the crystal structure of N-Ras bound to a GTP analogue and interpret the kinetic data in terms of structural features specific for H-, K-, and N-Ras.

PubMed: 28630043
DOI: 10.1074/jbc.M117.778886

実験手法

X-RAY DIFFRACTION (1.672 Å)