RGS9-Gβ5 substrate selectivity in photoreceptors: Opposing effects of constituent domains yield high affinity of RGS interaction with the G protein-effector complex

Journal of Biological Chemistry

Volumn 276, Issue 40, 2001, Pages 37365-37372

  Skiba, Nikolai P ^a   Martemyanov, Kirill A ^a   Elfenbein, Arye ^a   Hopp, Johnathan A ^a   Bohm, Andrew ^b,c   Simonds, William F ^d   Arshavsky, Vadim Y ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

^c TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; HYDROLYSIS; PROTEINS; SUBSTRATES;

PHOTORECEPTORS; PROTEIN SIGNALING;

BIOCHEMISTRY;

CYCLIC GMP PHOSPHODIESTERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN BETA5 SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; RGS PROTEIN; RGS9 GUANINE NUCLEOTIDE BINDING PROTEIN BETA5 SUBUNIT COMPLEX; RGS9 PROTEIN; TRANSDUCIN; UNCLASSIFIED DRUG; GAMMA SUBUNIT, CGMP PHOSPHODIESTERASE; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; REGULATOR OF G PROTEIN SIGNALING 9; REGULATOR OF G-PROTEIN SIGNALING 9;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CATALYSIS; CATTLE; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; ENZYME ACTIVATION; ENZYME ACTIVITY; HYDROLYSIS; NONHUMAN; PHOTORECEPTOR; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; ANIMAL; ENZYME SPECIFICITY; KINETICS; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

ANIMALIA; BOS TAURUS;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; ANIMALS; CATALYSIS; CATTLE; GTP-BINDING PROTEIN BETA SUBUNITS; HETEROTRIMERIC GTP-BINDING PROTEINS; KINETICS; PHOTORECEPTORS; PROTEIN STRUCTURE, TERTIARY; RGS PROTEINS; SUBSTRATE SPECIFICITY; TRANSDUCIN;

EID: 0035813162     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M106431200     Document Type: Article

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