Phosphorylation of isolated human phosphodiesterase-5 regulatory domain induces an apparent conformational change and increases cGMP binding affinity

Journal of Biological Chemistry

Volumn 277, Issue 49, 2002, Pages 47581-47587

  Francis, Sharron H ^a   Bessay, Emmanuel P ^a   Kotera, Jun ^a   Grimes, Kennard A ^a   Liu, Li ^b,c   Joseph Thompson, W ^b,c   Corbin, Jackie D ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF SOUTH ALABAMA COLLEGE OF MEDICINE   (United States)

^c Cell Pathways Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; STOICHIOMETRY;

PHOSPHORYLATIONS;

BIOCHEMISTRY;

CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP; CYCLIC NUCLEOTIDE DEPENDENT PROTEIN KINASE; PEPTIDE FRAGMENT; PHOSPHODIESTERASE V; POLYACRYLAMIDE GEL; PROTEIN; SERINE; UNCLASSIFIED DRUG; VALYLGLUTAMIC ACID;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; STOICHIOMETRY;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; ALLOSTERIC SITE; BINDING SITES; CATALYSIS; CYCLIC GMP; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; PHOSPHORIC DIESTER HYDROLASES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; TIME FACTORS;

EID: 0037033002     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206088200     Document Type: Article

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