Structural highlights
Publication Abstract from PubMed
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.
Structural biology of human cannabinoid receptor-2 helix 6 in membrane-mimetic environments.,Tiburu EK, Tyukhtenko S, Deshmukh L, Vinogradova O, Janero DR, Makriyannis A Biochem Biophys Res Commun. 2009 Jun 26;384(2):243-8. Epub 2009 May 3. PMID:19397896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tiburu EK, Tyukhtenko S, Deshmukh L, Vinogradova O, Janero DR, Makriyannis A. Structural biology of human cannabinoid receptor-2 helix 6 in membrane-mimetic environments. Biochem Biophys Res Commun. 2009 Jun 26;384(2):243-8. Epub 2009 May 3. PMID:19397896 doi:10.1016/j.bbrc.2009.04.099
