Is the function of the cdc2 kinase subunit proteins tuned by their propensities to oligomerize? Conformational states in solution of the cdc2 kinase partners p13sucland p9cksphy

Biochemistry

Volumn 35, Issue 17, 1996, Pages 5577-5585

  Birck, Catherine ^a   Vachette, Patrice ^a,b   Welch, Martin ^a   Swarén, Peter ^a   Samama, Jean Pierre ^a  

^a Lab Pharmacologie/Toxicologie F   (France)

^b UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE;

ARTICLE; ENZYME CONFORMATION; ENZYME SUBUNIT; MITOSIS; NONHUMAN; OLIGOMERIZATION; PHYSARUM POLYCEPHALUM; PRIORITY JOURNAL; SCHIZOSACCHAROMYCES POMBE;

AMINO ACID SEQUENCE; ANIMALS; CDC2 PROTEIN KINASE; CELL CYCLE PROTEINS; FUNGAL PROTEINS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHYSARUM POLYCEPHALUM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTOZOAN PROTEINS; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; X-RAYS;

EID: 0030008233     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952199b     Document Type: Article

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