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TitleMEK drives BRAF activation through allosteric control of KSR proteins.
Journal, issue, pagesNature, Vol. 554, Page 549-553, Year 2018
Publish dateMay 10, 2017 (structure data deposition date)
AuthorsLavoie, H. / Sahmi, M. / Maisonneuve, P. / Marullo, S.A. / Thevakumaran, N. / Jin, T. / Kurinov, I. / Sicheri, F. / Therrien, M.
External linksNature / PubMed:29433126
MethodsX-ray diffraction
Resolution1.749 - 2.102 Å
Structure data

PDB-5vr3:
Crystal structure of the BRS domain of BRAF
Method: X-RAY DIFFRACTION / Resolution: 2.102 Å

PDB-5vyk:
Crystal structure of the BRS domain of BRAF in complex with the CC-SAM domain of KSR1
Method: X-RAY DIFFRACTION / Resolution: 1.749 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / BRAF / SIGNALING PROTEIN / KSR1 / BRS / CC-SAM / Complex / Kinase / Pseudokinase / Signaling.

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