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TitleStructural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2.
Journal, issue, pagesBiochemistry, Vol. 55, Page 2269-2277, Year 2016
Publish dateFeb 16, 2016 (structure data deposition date)
AuthorsLaRochelle, J.R. / Fodor, M. / Xu, X. / Durzynska, I. / Fan, L. / Stams, T. / Chan, H.M. / LaMarche, M.J. / Chopra, R. / Wang, P. ...LaRochelle, J.R. / Fodor, M. / Xu, X. / Durzynska, I. / Fan, L. / Stams, T. / Chan, H.M. / LaMarche, M.J. / Chopra, R. / Wang, P. / Fortin, P.D. / Acker, M.G. / Blacklow, S.C.
External linksBiochemistry / PubMed:27030275
MethodsX-ray diffraction
Resolution1.87 - 2.32 Å
Structure data

PDB-5i6v:
Structure of F285S, a Cancer-Associated Mutation of the Oncogenic Phosphatase SHP2
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-5ibm:
Structure of S502P, a Cancer-Associated Mutation of the Oncogenic Phosphatase SHP2
Method: X-RAY DIFFRACTION / Resolution: 2.18 Å

PDB-5ibs:
Structure of E76Q, a Cancer-Associated Mutation of the Oncogenic Phosphatase SHP2
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / SHP2 / Cancer-Associated Mutation / Inhibitors / TYROSINE PHOSPHATASE SHP2 S502P / Tyrosine-protein phosphatase non-receptor type 11 / TYROSINE PHOSPHATASE SHP2

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