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TitleAn allosteric site on MKP5 reveals a strategy for small-molecule inhibition.
Journal, issue, pagesSci. Signal., Vol. 13, Year 2020
Publish dateAug 30, 2018 (structure data deposition date)
AuthorsGannam, Z.T.K. / Min, K. / Shillingford, S.R. / Zhang, L. / Herrington, J. / Abriola, L. / Gareiss, P.C. / Pantouris, G. / Tzouvelekis, A. / Kaminski, N. ...Gannam, Z.T.K. / Min, K. / Shillingford, S.R. / Zhang, L. / Herrington, J. / Abriola, L. / Gareiss, P.C. / Pantouris, G. / Tzouvelekis, A. / Kaminski, N. / Zhang, X. / Yu, J. / Jamali, H. / Ellman, J.A. / Lolis, E. / Anderson, K.S. / Bennett, A.M.
External linksSci. Signal. / PubMed:32843541
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-6mc1:
Structure of MAP kinase phosphatase 5 in complex with 3,3-dimethyl-1-((9-(methylthio)-5,6-dihydrothieno[3,4-h]quinazolin-2-yl)thio)butan-2-one, an allosteric inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-CJA:
3,3-dimethyl-1-{[9-(methylsulfanyl)-5,6-dihydrothieno[3,4-h]quinazolin-2-yl]sulfanyl}butan-2-one

ChemComp-DTT:
2,3-DIHYDROXY-1,4-DITHIOBUTANE

ChemComp-ACT:
ACETATE ION

Source
  • homo sapiens (human)
KeywordsHydrolase/Hydrolase Inhibitor / phosphatase / protein-tyrosine phosphatase / dual specificity phosphatase / phosphatase-inhibitor complex / HYDROLASE-HYDROLASE Inhibitor complex

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