The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis

Biochemistry

Volumn 42, Issue 45, 2003, Pages 13220-13226

  Huai, Qing ^a   Colicelli, John ^b   Ke, Hengming ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; DISEASES; HYDROLYSIS; WATER;

INTRACELLULAR CONCENTRATIONS;

ENZYMES;

ADENOSINE PHOSPHATE; ANTIASTHMATIC AGENT; ANTICOAGULANT AGENT; ANTIDEPRESSANT AGENT; CARDIOTONIC AGENT; CILOSTAZOL; CYCLIC AMP; CYCLIC GMP; HYDROXIDE; METAL ION; PHOSPHATE; PHOSPHODIESTERASE INHIBITOR; PHOSPHODIESTERASE IV; SILDENAFIL; SPASMOLYTIC AGENT; VASODILATOR AGENT; WATER;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; PRIORITY JOURNAL;

3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; ADENOSINE MONOPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CATIONS, DIVALENT; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROLYSIS; METALS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS;

EID: 0242401840     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034653e     Document Type: Article

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