| Literature DB >> 19397896 |
Elvis K Tiburu1, Sergiy Tyukhtenko, Lalit Deshmukh, Olga Vinogradova, David R Janero, Alexandros Makriyannis.
Abstract
We detail the structure and dynamics of a synthetic peptide corresponding to transmembrane helix 6 (TMH6) of human cannabinoid receptor-2 (hCB2) in biomembrane-mimetic environments. The peptide's NMR structural biology is characterized by two alpha-helical domains bridged by a flexible, nonhelical hinge region containing a highly-conserved CWFP motif with an environmentally sensitive, Pro-based conformational switch. Buried within the peptide's flexible region, W(258) may hydrogen-bond with L(255) to help stabilize the Pro-kinked hCB2 TMH6 structure and position C(257) advantageously for interaction with agonist ligands. These characteristics of hCB2 TMH6 are potential structural features of ligand-induced hCB2 activation in vivo.Entities:
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Year: 2009 PMID: 19397896 PMCID: PMC3679894 DOI: 10.1016/j.bbrc.2009.04.099
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575