UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions

Journal of Biological Chemistry

Volumn 275, Issue 14, 2000, Pages 10349-10358

  Beard, Matthew B ^a   Olsen, Aileen E ^b   Jones, Randy E ^b   Erdogan, Suat ^a,c   Houslay, Miles D ^a   Bolger, Graeme B ^b,d  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b UNIVERSITY OF UTAH HEALTH SCIENCES CENTER   (United States)

^c MUSTAFA KEMAL UNIVERSITY   (Turkey)

^d VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLIC AMP; PHOSPHODIESTERASE; PROTEIN KINASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; GENE DISRUPTION; GENE LOCATION; GENE MUTATION; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN ISOLATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION;

3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYTIC DOMAIN; CLONING, MOLECULAR; CONSERVED SEQUENCE; DNA, COMPLEMENTARY; ELECTROSTATICS; HELA CELLS; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA;

EID: 0034616226     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.14.10349     Document Type: Article

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