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Structure paper

TitleMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2.
Journal, issue, pagesNat Commun, Vol. 9, Page 4507-4507, Year 2018
Publish dateMar 6, 2018 (structure data deposition date)
AuthorsPadua, R.A.P. / Sun, Y. / Marko, I. / Pitsawong, W. / Stiller, J.B. / Otten, R. / Kern, D.
External linksNat Commun / PubMed:30375376
MethodsX-ray diffraction
Resolution1.8 - 2.9 Å
Structure data

PDB-6cmp:
Closed structure of inactive SHP2 mutant C459E
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6cmq:
Structure of human SHP2 without N-SH2 domain
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-6cmr:
Closed structure of active SHP2 mutant E76D bound to SHP099 inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.21 Å

PDB-6cms:
Closed structure of active SHP2 mutant E76K bound to SHP099 inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.68 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-5OD:
6-(4-azanyl-4-methyl-piperidin-1-yl)-3-[2,3-bis(chloranyl)phenyl]pyrazin-2-amine

Source
  • homo sapiens (human)
KeywordsHYDROLASE / protein tyrosine phosphatase / src homology domain 2 / inactive state / inactive mutant / open state / active mutant / HYDROLASE/HYDROLASE Inhibitor / HYDROLASE-HYDROLASE Inhibitor complex

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