Structural and functional features in human PDE5A1 regulatory domain that provide for allosteric cGMP binding, dimerization, and regulation

Journal of Biological Chemistry

Volumn 280, Issue 12, 2005, Pages 12051-12063

  Zoraghi, Roya ^a   Bessay, Emmanuel P ^a   Corbin, Jackie D ^a   Francis, Sharron H ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; DIMERIZATION; DIMERS; ESCHERICHIA COLI; REACTION KINETICS; STRUCTURE (COMPOSITION);

ANABAENA ADENYLYL CYCLASES; CATALYTIC DOMAIN; HUMAN PDE5A1 REGULATORY DOMAIN; QUATERNARY STRUCTURES;

ENZYMES;

CYCLIC GMP; CYCLIC NUCLEOTIDE DEPENDENT PROTEIN KINASE; HOLOENZYME; PHOSPHODIESTERASE V;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; DIMERIZATION; DISSOCIATION; DNA FLANKING REGION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME PURIFICATION; ENZYME REGULATION; ENZYME STABILITY; GENETIC HETEROGENEITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN QUATERNARY STRUCTURE;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; ALLOSTERIC REGULATION; AMINO ACID MOTIFS; CATALYTIC DOMAIN; CYCLIC AMP; CYCLIC GMP; DIMERIZATION; HUMANS; PHOSPHORYLATION; PROTEIN CONFORMATION;

ANABAENA; ESCHERICHIA COLI; MAMMALIA;

EID: 15744369740     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M413611200     Document Type: Article

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