9C1B
Crystal structure of GDP-bound human M-RAS protein in crystal form II
Summary for 9C1B
| Entry DOI | 10.2210/pdb9c1b/pdb |
| Related | 9C1A |
| Descriptor | Ras-related protein M-Ras, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | m-ras, gdp, gtpase structure, ras, crystal packing, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 103964.68 |
| Authors | Bester, S.M.,Abrahamsen, R.,Samora, L.R.,Wu, W.-I.,Mou, T.-C. (deposition date: 2024-05-28, release date: 2024-09-11, Last modification date: 2024-09-18) |
| Primary citation | Bester, S.M.,Abrahamsen, R.,Rodrigues Samora, L.,Wu, W.I.,Mou, T.C. Crystal structure of the GDP-bound human M-RAS protein in two crystal forms. Acta Crystallogr.,Sect.F, 80:220-227, 2024 Cited by PubMed Abstract: M-RAS plays a crucial role in the RAF-MEK signaling pathway. When activated by GTP, M-RAS forms a complex with SHOC2 and PP1C, initiating downstream RAF-MEK signal transduction. In this study, the crystal structure of the GDP-bound human M-RAS protein is presented with two forms of crystal packing. Both the full-length and truncated human M-RAS structures aligned well with the high-confidence section of the AlphaFold2-predicted structure with low r.m.s.d., except for the Switch regions. Despite high sequence similarity to the available mouse M-RAS structure, the full-length human M-RAS structure exhibits unique crystal packing. This inactive human M-RAS structure could offer novel insights for the design of selective compounds targeting M-RAS. PubMed: 39196705DOI: 10.1107/S2053230X24007969 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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