7JHP
Crystal structure of HRas in complex with the Ras-binding and cysteine-rich domains of CRaf-kinase
Summary for 7JHP
| Entry DOI | 10.2210/pdb7jhp/pdb |
| Descriptor | GTPase HRas, RAF proto-oncogene serine/threonine-protein kinase, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (6 entities in total) |
| Functional Keywords | ras, raf, rbd, crd, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 34862.48 |
| Authors | Cookis, T.,Mattos, C. (deposition date: 2020-07-21, release date: 2020-08-05, Last modification date: 2023-10-18) |
| Primary citation | Cookis, T.,Mattos, C. Crystal Structure Reveals the Full Ras-Raf Interface and Advances Mechanistic Understanding of Raf Activation. Biomolecules, 11:-, 2021 Cited by PubMed Abstract: Ras and Raf-kinase interact through the Ras-binding (RBD) and cysteine-rich domains (CRD) of Raf to signal through the mitogen-activated protein kinase pathway, yet the molecular mechanism leading to Raf activation has remained elusive. We present the 2.8 Å crystal structure of the HRas-CRaf-RBD_CRD complex showing the Ras-Raf interface as a continuous surface on Ras, as seen in the KRas-CRaf-RBD_CRD structure. In molecular dynamics simulations of a Ras dimer model formed through the α4-α5 interface, the CRD is dynamic and located between the two Ras protomers, poised for direct or allosteric modulation of functionally relevant regions of Ras and Raf. We propose a molecular model in which Ras binding is involved in the release of Raf autoinhibition while the Ras-Raf complex dimerizes to promote a platform for signal amplification, with Raf-CRD centrally located to impact regulation and function. PubMed: 34356620DOI: 10.3390/biom11070996 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.766 Å) |
Structure validation
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