The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase

EMBO Journal

Volumn 22, Issue 14, 2003, Pages 3524-3535

  Gray, Christopher H ^a   Good, Valerie M ^a   Tonks, Nicholas K ^b   Barford, David ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

Author keywords

Cdc14 dual specificity phosphatase proline directed phosphatase protein structure X ray crystallography

Indexed keywords

CELL CYCLE PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROLINE; PROTEIN CDC14; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DEPHOSPHORYLATION; DOWN REGULATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; EUKARYOTE; MITOSIS; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CELL CYCLE PROTEINS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEIN PHOSPHATASE; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE-PHOSPHATASE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EUKARYOTA;

EID: 0041312681     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg348     Document Type: Article

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