Crystal structure of the cytoplasmic phosphatase and tensin homolog (PTEN)-like region of Ciona intestinalis voltage-sensing phosphatase provides insight into substrate specificity and redox regulation of the phosphoinositide phosphatase activity

Journal of Biological Chemistry

Volumn 286, Issue 26, 2011, Pages 23368-23377

  Matsuda, Makoto ^a   Takeshita, Kohei ^a   Kurokawa, Tatsuki ^a   Sakata, Souhei ^a   Suzuki, Mamoru ^a   Yamashita, Eiki ^a   Okamura, Yasushi ^a   Nakagawa, Atsushi ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

5-BISPHOSPHATE; ACTIVE SITE; ACTIVE SITE POCKET; CATALYTIC RESIDUE; CYTOPLASMIC REGIONS; DEPHOSPHORYLATES; DISULFIDE BONDS; ENZYMATIC MECHANISMS; GLUTAMIC ACID; INTERACTION DOMAIN; MEMBRANE DEPOLARIZATION; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4 ,5-BISPHOSPHATE; PHOSPHOINOSITIDE PHOSPHATASE; REACTIVE OXYGEN SPECIES; REDOX REGULATION; SUBSTRATE SPECIFICITY; TRANSMEMBRANE VOLTAGE; WILD TYPES;

AMINO ACIDS; COVALENT BONDS; PHOSPHATASES;

CRYSTAL STRUCTURE;

GLUTAMIC ACID; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOINOSITIDE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VOLTAGE SENSING PHOSPHATASE;

ARTICLE; CATALYSIS; CIONA INTESTINALIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASM; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SPECIFICITY; GENE MUTATION; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; WILD TYPE;

AMINO ACID SUBSTITUTION; ANIMALS; CATALYTIC DOMAIN; CIONA INTESTINALIS; CRYSTALLOGRAPHY, X-RAY; MUTATION, MISSENSE; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PTEN PHOSPHOHYDROLASE; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

CIONA INTESTINALIS;

EID: 79959560819     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.214361     Document Type: Article

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