2PBI
The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure
Summary for 2PBI
| Entry DOI | 10.2210/pdb2pbi/pdb |
| Descriptor | Regulator of G-protein signaling 9, Guanine nucleotide-binding protein subunit beta 5, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | helix wrap, rgs domain, dep domain, dhex domain, ggl domain, beta propeller, signaling protein |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Membrane : P62881 |
| Total number of polymer chains | 4 |
| Total formula weight | 178380.53 |
| Authors | Cheever, M.L.,Snyder, J.T.,Gershburg, S.,Siderovski, D.P.,Harden, T.K.,Sondek, J. (deposition date: 2007-03-28, release date: 2008-01-29, Last modification date: 2024-02-21) |
| Primary citation | Cheever, M.L.,Snyder, J.T.,Gershburg, S.,Siderovski, D.P.,Harden, T.K.,Sondek, J. Crystal structure of the multifunctional Gbeta5-RGS9 complex. Nat.Struct.Mol.Biol., 15:155-162, 2008 Cited by PubMed Abstract: Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (Galpha) subunits and are vital for proper signaling kinetics downstream of G protein-coupled receptors (GPCRs). R7 subfamily RGS proteins specifically and obligately dimerize with the atypical G protein beta5 (Gbeta5) subunit through an internal G protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the 1.95-A crystal structure of the Gbeta5-RGS9 complex, which is essential for normal visual and neuronal signal transduction. This structure reveals a canonical RGS domain that is functionally integrated within a molecular complex that is poised for integration of multiple steps during G-protein activation and deactivation. PubMed: 18204463DOI: 10.1038/nsmb.1377 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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