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TitleModification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding.
Journal, issue, pagesBiochem. J., Vol. 465, Page 149-161, Year 2015
Publish dateFeb 3, 2015 (structure data deposition date)
AuthorsVisperas, P.R. / Winger, J.A. / Horton, T.M. / Shah, N.H. / Aum, D.J. / Tao, A. / Barros, T. / Yan, Q. / Wilson, C.G. / Arkin, M.R. ...Visperas, P.R. / Winger, J.A. / Horton, T.M. / Shah, N.H. / Aum, D.J. / Tao, A. / Barros, T. / Yan, Q. / Wilson, C.G. / Arkin, M.R. / Weiss, A. / Kuriyan, J.
External linksBiochem. J. / PubMed:25287889
MethodsX-ray diffraction
Resolution2 - 2.8 Å
Structure data

PDB-4xz0:
ZAP-70-tSH2:compound-A complex
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4xz1:
ZAP-70-tSH2:Compound-B adduct
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-4N5:
1-(3-{5-[(3-chlorobenzyl)sulfonyl]-1H-tetrazol-1-yl}phenyl)ethanone

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-4N6:
2-[(7-chloro-4-nitro-2,1,3-benzoxadiazol-5-yl)amino]ethanol

Source
  • homo sapiens (human)
KeywordsTransferase/Transferase inhibitor / Tyrosine kinase / cysteine adduct / Transferase-Transferase inhibitor complex

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