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8CPD

Cryo-EM structure of CRaf dimer with 14:3:3

Summary for 8CPD
Entry DOI10.2210/pdb8cpd/pdb
Related8chf
EMDB information16779
DescriptorRAF proto-oncogene serine/threonine-protein kinase, 14-3-3 protein zeta isoform X1 (2 entities in total)
Functional Keywordskinase, complex, cytokine
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight202585.98
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 citationDedden, 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: 38331211
DOI: 10.1016/j.jmb.2024.168483
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.46 Å)
Structure validation

237735

数据于2025-06-18公开中

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