4EFM
Crystal structure of H-Ras G12V in complex with GppNHp (state 1)
Summary for 4EFM
| Entry DOI | 10.2210/pdb4efm/pdb |
| Related | 1XCM 3KKN 4EFL 4EFN |
| Descriptor | GTPase HRas, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rossmann fold, gtpase, gtp-binding, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane. Isoform 2: Nucleus: P01112 |
| Total number of polymer chains | 1 |
| Total formula weight | 19875.23 |
| Authors | Muraoka, S.,Shima, F.,Araki, M.,Inoue, T.,Yoshimoto, A.,Ijiri, Y.,Seki, N.,Tamura, A.,Kumasaka, T.,Yamamoto, M.,Kataoka, T. (deposition date: 2012-03-30, release date: 2012-05-16, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 22584058DOI: 10.1016/j.febslet.2012.04.058 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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