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Structure paper

TitleToward the Rational Design of P53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant.
Journal, issue, pagesChem. Biol., Vol. 17, Page 46-, Year 2010
Publish dateDec 17, 2009 (structure data deposition date)
AuthorsBasse, N. / Kaar, J.L. / Settanni, G. / Joerger, A.C. / Rutherford, T.J. / Fersht, A.R.
External linksChem. Biol. / PubMed:20142040
MethodsX-ray diffraction
Resolution1.6 - 2.1 Å
Structure data

PDB-2x0u:
STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO A 2-amino substituted benzothiazole scaffold
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-2x0v:
STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 4-(trifluoromethyl)benzene-1,2-diamine
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2x0w:
STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 5,6-dimethoxy- 2-methylbenzothiazole
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-X0U:
6,7-DIHYDRO[1,4]DIOXINO[2,3-F][1,3]BENZOTHIAZOL-2-AMINE

ChemComp-HOH:
WATER

ChemComp-X0V:
4-(TRIFLUOROMETHYL)BENZENE-1,2-DIAMINE

ChemComp-X0W:
5,6-DIMETHOXY-2-METHYL-1,3-BENZOTHIAZOLE

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / ACTIVATOR / TRANSCRIPTION REGULATION / TRANSCRIPTION FACTOR / LI-FRAUMENI DRUG DISCOVERY / SURFACE CREVICE / TUMOR SUPPRESSOR / PROTEIN STABILIZATION / TRANSCRIPTION / METAL BINDING / CANCER / APOPTOSIS / HOST-VIRUS INTERACTION / LI-FRAUMENI SYNDROME / DRUG DISCOVERY

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