BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain

Journal of Biological Chemistry

Volumn 285, Issue 5, 2010, Pages 3439-3450

  Hagn, Franz ^a   Klein, Christian ^b   Demmer, Oliver ^a   Marchenko, Natasha ^c   Vaseva, Angelina ^c   Moll, Ute M ^c   Kessler, Horst ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b ROCHE DIAGNOSTICS GMBH   (Germany)

^c STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-APOPTOTIC PROTEIN; APOPTOSIS; BINDING BEHAVIORS; DNA BINDING; DNA BINDING DOMAIN; FLUORESCENCE POLARIZATION; MITOCHONDRIAL MEMBRANES; MODE OF ACTION; NMR SPECTROSCOPY; PRO-APOPTOTIC FUNCTION; PROTEIN-LIGAND COMPLEXES; PROTEIN-PROTEIN COMPLEXES; RATIONAL DESIGN; RESIDUAL DIPOLAR COUPLINGS; SMALL MOLECULE INHIBITOR; STRUCTURAL CHANGE; STRUCTURAL MODELS; WILD TYPES;

CELL DEATH; CELL MEMBRANES; DNA; GENES; MITOCHONDRIA; MODEL STRUCTURES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

COMPLEXATION;

BINDING PROTEIN; PIFITHRIN MU; PROTEIN BCL XL; PROTEIN P53; UNCLASSIFIED DRUG; 2 PHENYLACETYLENESULFONAMIDE; 2-PHENYLACETYLENESULFONAMIDE; DNA; LIGAND; PROTEIN BCL X; SULFONAMIDE; TP53 PROTEIN, HUMAN;

ALLOSTERISM; APOPTOSIS; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE POLARIZATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MITOCHONDRION; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; BINDING SITE; CHEMISTRY; CONFORMATION; METHODOLOGY; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY; TUMOR SUPPRESSOR GENE;

ALLOSTERIC SITE; BCL-X PROTEIN; DNA; GENES, P53; HUMANS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SULFONAMIDES; TUMOR SUPPRESSOR PROTEIN P53;

EID: 77449091505     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.065391     Document Type: Article

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