1lvq

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lvq OCA], [https://pdbe.org/1lvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lvq RCSB], [https://www.ebi.ac.uk/pdbsum/1lvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lvq ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

Cannabinoid receptor-G protein interactions: G(alphai1)-bound structures of IC3 and a mutant with altered G protein specificity.,Ulfers AL, McMurry JL, Miller A, Wang L, Kendall DA, Mierke DF Protein Sci. 2002 Oct;11(10):2526-31. PMID:12237474<ref>PMID:12237474</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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