1TND
THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S
Summary for 1TND
Entry DOI | 10.2210/pdb1tnd/pdb |
Descriptor | TRANSDUCIN, MAGNESIUM ION, CACODYLATE ION, ... (5 entities in total) |
Functional Keywords | binding protein(gtp) |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 3 |
Total formula weight | 113936.98 |
Authors | Noel, J.P.,Hamm, H.E.,Sigler, P.B. (deposition date: 1994-03-31, release date: 1994-07-31, Last modification date: 2024-02-14) |
Primary citation | Noel, J.P.,Hamm, H.E.,Sigler, P.B. The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S. Nature, 366:654-663, 1993 Cited by PubMed Abstract: The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data. PubMed: 8259210DOI: 10.1038/366654a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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