Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα)·GTPγΣ

Science

Volumn 278, Issue 5345, 1997, Pages 1907-1916

  Tesmer, John J G ^a   Sunahara, Roger K ^b   Gilman, Alfred G ^b   Sprang, Stephen R ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CATALYSTS; CHEMICAL ACTIVATION; CRYSTAL STRUCTURE; ENZYME INHIBITION; MOLECULAR DYNAMICS; PROTEINS;

ADENYLYL CYCLASE; FORSKOLIN; HETEROTRIMERIC G PROTEIN;

ENZYMES;

ADENYLATE CYCLASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE);

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; MAMMAL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME ACTIVATION; FORSKOLIN; GTP-BINDING PROTEIN ALPHA SUBUNITS, GS; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

MAMMALIA;

EID: 2642689663     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5345.1907     Document Type: Article

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56. 2 homodimer before their release in the Protein Data Bank; R. Johnson for supplying 2′-deoxy-3′-ATP (synthesis supported by NIH grant DK38828); and R. Cooke for supplying 2′-iodo-ATP. Supported by NIH grant DK46371 and Welch Foundation grant I-1229 to S.R.S.; by NIH grant GM34497, American Cancer Society grant RPG-77-001-21-BE, Welch Foundation grant I-1271, and the Raymond and Ellen Willie Distinguished Chair of Molecular Neuropharmacology to A.G.G; and a post-doctoral fellowship from the Medical Research Council of Canada to R.K.S. Atomic coordinates have been submitted to the Protein Data Bank (1AZS).