Publication Date:
1998-01-07
Description:
The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tesmer, J J -- Sunahara, R K -- Gilman, A G -- Sprang, S R -- DK38828/DK/NIDDK NIH HHS/ -- DK46371/DK/NIDDK NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1907-16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417641" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/metabolism
;
Adenylyl Cyclase Inhibitors
;
Adenylyl Cyclases/*chemistry/metabolism
;
Amino Acid Sequence
;
Binding Sites
;
Catalysis
;
Colforsin/metabolism
;
Crystallization
;
Crystallography, X-Ray
;
Dimerization
;
Enzyme Activation
;
GTP-Binding Protein alpha Subunits, Gs/*chemistry/metabolism
;
Guanosine 5'-O-(3-Thiotriphosphate)/*chemistry/metabolism
;
Ligands
;
Models, Molecular
;
Molecular Sequence Data
;
Mutation
;
Phosphorylation
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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