1GOT
HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS
Summary for 1GOT
| Entry DOI | 10.2210/pdb1got/pdb |
| Descriptor | GT-ALPHA/GI-ALPHA CHIMERA, GT-BETA, GT-GAMMA, ... (5 entities in total) |
| Functional Keywords | complex (gtp-binding-transducer), g protein, heterotrimer signal transduction, complex (gtp-binding-transducer) complex, complex (gtp-binding/transducer) |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P02698 |
| Total number of polymer chains | 3 |
| Total formula weight | 87138.46 |
| Authors | Lambright, D.G.,Sondek, J.,Bohm, A.,Skiba, N.P.,Hamm, H.E.,Sigler, P.B. (deposition date: 1996-08-07, release date: 1997-03-12, Last modification date: 2024-10-16) |
| Primary citation | Lambright, D.G.,Sondek, J.,Bohm, A.,Skiba, N.P.,Hamm, H.E.,Sigler, P.B. The 2.0 A crystal structure of a heterotrimeric G protein. Nature, 379:311-319, 1996 Cited by PubMed Abstract: The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor. PubMed: 8552184DOI: 10.1038/379311a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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