The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53

Journal of Biological Chemistry

Volumn 282, Issue 15, 2007, Pages 11300-11307

  Kaustov, Lilia ^a   Lukin, Jonathan ^a,b   Lemak, Alexander ^a,b   Duan, Shili ^a   Ho, Melissa ^a   Doherty, Ryan ^a   Penn, Linda Z ^a   Arrowsmith, Cheryl H ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c TMDT   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CELLS; CHROMATOGRAPHIC ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

CULLIN RING LIGASE (CRL); PEPTIDE INTERACTIONS; PROTEIN-PROTEIN INTERACTIONS;

MOLECULAR INTERACTIONS;

PROTEIN P53; PROTEIN PARC; PROTEIN SUBUNIT; CARRIER PROTEIN; CUL7 PROTEIN, HUMAN; CULLIN; H7 AP1 PROTEIN, HUMAN; H7-AP1 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

ARTICLE; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MOLECULAR EVOLUTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PROTEIN MOTIF; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID MOTIFS; CARRIER PROTEINS; CONSERVED SEQUENCE; CULLIN PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 34249674388     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M611297200     Document Type: Article

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