Structural and functional characterization of the 2H-phosphatase domain of Sts-2 reveals an acid-dependent phosphatase activity

Biochemistry

Volumn 48, Issue 8, 2009, Pages 1681-1690

  Chen, Yunting ^a   Jakoncic, Jean ^b   Carpino, Nick ^c   Nassar, Nicolas ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

^c STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; ACTIVE SITES; CATALYTIC RESIDUES; EPIDERMAL GROWTH FACTOR RECEPTORS; FUNCTIONAL CHARACTERIZATIONS; HOMOLOGY DOMAINS; ISOFORMS; MEMBRANE-BOUND RECEPTORS; MODEL SUBSTRATES; MULTIDOMAIN PROTEINS; PHOSPHATASE ACTIVITIES; PHYSIOLOGICAL SUBSTRATES; PROTEIN-TYROSINE PHOSPHATASE; STRUCTURAL HOMOLOGIES; T CELLS; T-CELL RECEPTORS;

ACIDS; AMINO ACIDS; CELL GROWTH; CELL MEMBRANES; CRYSTAL STRUCTURE; ELECTRIC REACTORS; ENZYMES; SIGNALING; THERMAL CONDUCTIVITY OF SOLIDS; TUNGSTEN COMPOUNDS;

ENZYME ACTIVITY;

ACID PHOSPHATASE; CELL PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; MEMBRANE RECEPTOR; PHOSPHATE; PHOSPHOGLYCERATE MUTASE; PROTEIN TYROSINE PHOSPHATASE; STS 2 PROTEIN; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; T LYMPHOCYTE;

ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; INHIBITORY CONCENTRATION 50; KINETICS; MICE; MODELS, MOLECULAR; MUTANT PROTEINS; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, T-CELL; RECOMBINANT PROTEINS;

EID: 64349095418     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802219n     Document Type: Article

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