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TitleiASPP mediates p53 selectivity through a modular mechanism fine-tuning DNA recognition.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 17470-17479, Year 2019
Publish dateJun 12, 2019 (structure data deposition date)
AuthorsChen, S. / Wu, J. / Zhong, S. / Li, Y. / Zhang, P. / Ma, J. / Ren, J. / Tan, Y. / Wang, Y. / Au, K.F. ...Chen, S. / Wu, J. / Zhong, S. / Li, Y. / Zhang, P. / Ma, J. / Ren, J. / Tan, Y. / Wang, Y. / Au, K.F. / Siebold, C. / Bond, G.L. / Chen, Z. / Lu, M. / Jones, E.Y. / Lu, X.
External linksProc. Natl. Acad. Sci. USA / PubMed:31395738
MethodsX-ray diffraction
Resolution4.23 Å
Structure data

PDB-6rz3:
Crystal structure of a complex between the DNA-binding domain of p53 and the carboxyl-terminal conserved region of iASPP
Method: X-RAY DIFFRACTION / Resolution: 4.23 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsANTITUMOR PROTEIN / Complex / p53 / iASPP

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