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Biochem Biophys Res Commun. 2009 Jun 26;384(2):243-8. doi: 10.1016/j.bbrc.2009.04.099. Epub 2009 May 3.

Structural biology of human cannabinoid receptor-2 helix 6 in membrane-mimetic environments.

Author information

  • 1Center for Drug Discovery and Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115-5000, USA.

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.

PMID:
19397896
[PubMed - indexed for MEDLINE]
PMCID:
PMC3679894
Free PMC Article
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