8CPD
Cryo-EM structure of CRaf dimer with 14:3:3
Summary for 8CPD
Entry DOI | 10.2210/pdb8cpd/pdb |
Related | 8chf |
EMDB information | 16779 |
Descriptor | RAF proto-oncogene serine/threonine-protein kinase, 14-3-3 protein zeta isoform X1 (2 entities in total) |
Functional Keywords | kinase, complex, cytokine |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 202585.98 |
Authors | Dedden, D.,Graedler, U.,Schwarz, D.,Thomsen, M.,Leuthner, B.,Schneider, E.,Nitsche, J. (deposition date: 2023-03-02, release date: 2024-02-21, Last modification date: 2024-11-20) |
Primary citation | Dedden, D.,Nitsche, J.,Schneider, E.V.,Thomsen, M.,Schwarz, D.,Leuthner, B.,Gradler, U. Cryo-EM Structures of CRAF 2 /14-3-3 2 and CRAF 2 /14-3-3 2 /MEK1 2 Complexes. J.Mol.Biol., 436:168483-168483, 2024 Cited by PubMed Abstract: RAF protein kinases are essential effectors in the MAPK pathway and are important cancer drug targets. Structural understanding of RAF activation is so far based on cryo-electron microscopy (cryo-EM) and X-ray structures of BRAF in different conformational states as inactive or active complexes with KRAS, 14-3-3 and MEK1. In this study, we have solved the first cryo-EM structures of CRAF/14-3-3 at 3.4 Å resolution and CRAF/14-3-3/MEK1 at 4.2 Å resolution using CRAF kinase domain expressed as constitutively active Y340D/Y341D mutant in insect cells. The overall architecture of our CRAF/14-3-3 and CRAF/14-3-3/MEK1 cryo-EM structures is highly similar to corresponding BRAF structures in complex with 14-3-3 or 14-3-3/MEK1 and represent the activated dimeric RAF conformation. Our CRAF cryo-EM structures provide additional insights into structural understanding of the activated CRAF/14-3-3/MEK1 complex. PubMed: 38331211DOI: 10.1016/j.jmb.2024.168483 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.46 Å) |
Structure validation
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