1AZS
COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE
Summary for 1AZS
| Entry DOI | 10.2210/pdb1azs/pdb |
| Descriptor | VC1, IIC2, GS-ALPHA, ... (7 entities in total) |
| Functional Keywords | complex (lyase-hydrolase), hydrolase, signal transducing protein, cyclase, effector enzyme, complex (lyase-hydrolase) complex, complex (lyase/hydrolase) |
| Biological source | Canis lupus familiaris (dog) More |
| Cellular location | Membrane; Multi-pass membrane protein: P30803 P26769 Cell membrane; Lipid-anchor (By similarity): P04896 |
| Total number of polymer chains | 3 |
| Total formula weight | 96554.63 |
| Authors | Tesmer, J.J.G.,Sprang, S.R. (deposition date: 1997-11-20, release date: 1998-02-25, Last modification date: 2024-05-22) |
| Primary citation | Tesmer, J.J.,Sunahara, R.K.,Gilman, A.G.,Sprang, S.R. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Science, 278:1907-1916, 1997 Cited by PubMed Abstract: 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. PubMed: 9417641DOI: 10.1126/science.278.5345.1907 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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