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TitleSolvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53--a structural and combinatorial approach.
Journal, issue, pagesProteins, Vol. 71, Page 1670-1685, Year 2008
Publish dateAug 8, 2006 (structure data deposition date)
AuthorsMora, P. / Carbajo, R.J. / Pineda-Lucena, A. / Sanchez del Pino, M.M. / Perez-Paya, E.
External linksProteins / PubMed:18076077
MethodsNMR (solution)
Structure data

PDB-2j0z:
p53 tetramerization domain wild type
Method: SOLUTION NMR

PDB-2j10:
p53 tetramerization domain mutant T329F Q331K
Method: SOLUTION NMR

PDB-2j11:
p53 tetramerization domain mutant Y327S T329G Q331G
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / P53 / ZINC / ACTIVATOR / APOPTOSIS / WILD TYPE / CELL CYCLE / ACETYLATION / DNA-BINDING / POLYMORPHISM / TETRAMERIZATION DOMAIN / TRANSCRIPTION REGULATION / ANTI-ONCOGENE / NUCLEAR PROTEIN / PHOSPHORYLATION / LI-FRAUMENI SYNDROME / HOST-VIRUS INTERACTION / DISEASE MUTATION / ALTERNATIVE SPLICING / GLYCOPROTEIN / METAL-BINDING

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