Send to:

Choose Destination
See comment in PubMed Commons below
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.


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.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk