1LVR
IC3 of CB1 (L431A,A432L) Bound to G(alpha)i
Summary for 1LVR
| Entry DOI | 10.2210/pdb1lvr/pdb |
| Related | 1LVQ |
| Descriptor | Cannabinoid receptor 1 (1 entity in total) |
| Functional Keywords | intracellular loop 3 (ic3), cannabinoid 1 receptor (cb1), alpha domain of g protein i, transferred noes, signaling protein |
| Cellular location | Cell membrane; Multi-pass membrane protein: P21554 |
| Total number of polymer chains | 1 |
| Total formula weight | 1030.26 |
| Authors | Ulfers, A.L.,McMurry, J.L.,Miller, A.,Wang, L.,Kendall, D.A.,Mierke, D.F. (deposition date: 2002-05-29, release date: 2002-12-11, Last modification date: 2024-05-22) |
| Primary citation | Ulfers, A.L.,McMurry, J.L.,Miller, A.,Wang, L.,Kendall, D.A.,Mierke, D.F. Cannabinoid receptor-G protein interactions: G(alphai1)-bound structures of IC3 and a mutant with altered G protein specificity. Protein Sci., 11:2526-2531, 2002 Cited by PubMed Abstract: The structure of the C-terminal region of the third cytoplasmic loop (IC3) of the cannabinoid receptor one (CB1) bound to G(alphai1) has been determined using transferred nuclear Overhauser effects (NOEs). The wild-type IC3 sequence is helical when associated with G(alphai1). In contrast, a peptide containing the amino-acid inversion, Ala(341)-Leu(342) adopts a single turn. These findings correlate with the attenuated G(i) association of CB1 with the Ala(341)-Leu(342) mutation previously observed in vivo and the diminished stimulation of G(alphai1) GTPase activity by the corresponding peptide demonstrated in vitro here. These results, the first to report the structure of a GPCR domain while associated with G protein, imply the C-terminus of CB1 IC3, a region with high-sequence conservation among G-protein coupled receptors, must be helical for efficient coupling and activation of the G(i) protein. PubMed: 12237474DOI: 10.1110/ps.0218402 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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