4EFM

Crystal structure of H-Ras G12V in complex with GppNHp (state 1)

4EFM の概要

• エントリーDOI: 10.2210/pdb4efm/pdb
• 関連するPDBエントリー: 1XCM 3KKN 4EFL 4EFN
• 分子名称: GTPase HRas, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: rossmann fold, gtpase, gtp-binding, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane. Isoform 2: Nucleus: P01112
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19875.23

構造登録者

Muraoka, S.,Shima, F.,Araki, M.,Inoue, T.,Yoshimoto, A.,Ijiri, Y.,Seki, N.,Tamura, A.,Kumasaka, T.,Yamamoto, M.,Kataoka, T. (登録日: 2012-03-30, 公開日: 2012-05-16, 最終更新日: 2023-11-08)

主引用文献

Muraoka, S.,Shima, F.,Araki, M.,Inoue, T.,Yoshimoto, A.,Ijiri, Y.,Seki, N.,Tamura, A.,Kumasaka, T.,Yamamoto, M.,Kataoka, T.
Crystal structures of the state 1 conformations of the GTP-bound H-Ras protein and its oncogenic G12V and Q61L mutants
Febs Lett., 586:1715-1718, 2012

PubMed Abstract: GTP-bound Ras adopts two interconverting conformations, "inactive" state 1 and "active" state 2. However, the tertiary structure of wild-type (WT) state 1 remains unsolved. Here we solve the state 1 crystal structures of H-Ras WT together with its oncogenic G12V and Q61L mutants. They assume open structures characterized by impaired interactions of both Thr-35 in switch I and Gly-60 in switch II with the γ-phosphate of GTP and possess two surface pockets of mutually different shapes unseen in state 2, a potential target for selective inhibitor development. Furthermore, they provide a structural basis for the low GTPase activity of state 1.

PubMed: 22584058
DOI: 10.1016/j.febslet.2012.04.058

実験手法

X-RAY DIFFRACTION (1.9 Å)