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TitleStructure-Reactivity Studies of 2-Sulfonylpyrimidines Allow Selective Protein Arylation.
Journal, issue, pagesBioconjug. Chem., Vol. 34, Page 1679-1687, Year 2023
Publish dateFeb 3, 2023 (structure data deposition date)
AuthorsPichon, M.M. / Drelinkiewicz, D. / Lozano, D. / Moraru, R. / Hayward, L.J. / Jones, M. / McCoy, M.A. / Allstrum-Graves, S. / Balourdas, D.I. / Joerger, A.C. ...Pichon, M.M. / Drelinkiewicz, D. / Lozano, D. / Moraru, R. / Hayward, L.J. / Jones, M. / McCoy, M.A. / Allstrum-Graves, S. / Balourdas, D.I. / Joerger, A.C. / Whitby, R.J. / Goldup, S.M. / Wells, N. / Langley, G.J. / Herniman, J.M. / Baud, M.G.J.
External linksBioconjug. Chem. / PubMed:37657082
MethodsX-ray diffraction
Resolution1.53 Å
Structure data

PDB-8cg7:
Structure of p53 cancer mutant Y220C with arylation at Cys182 and Cys277
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

Chemicals

ChemComp-ZN:
Unknown entry

PDB-1ih3:
Multi-conformation crystal structure of GGm5CGm5CC

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / p53 cancer mutation / protein stability / covalent modification / Cys-arylation

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