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

Elvis K. Tiburu, Sergiy Tyukhtenko, Lalit Deshmukh, Olga Vinogradova, David R. Janero, Alexandros Makriyannis

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

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 α-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, W258 may hydrogen-bond with L255 to help stabilize the Pro-kinked hCB2 TMH6 structure and position C257 advantageously for interaction with agonist ligands. These characteristics of hCB2 TMH6 are potential structural features of ligand-induced hCB2 activation in vivo.

Original languageEnglish
Pages (from-to)243-248
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume384
Issue number2
DOIs
Publication statusPublished - 26 Jun 2009
Externally publishedYes

Keywords

  • Agonist ligand
  • Conformational switch
  • G protein-coupled receptor
  • High-resolution NMR
  • Peptide helix
  • Proline
  • Spectrofluorometry
  • Structural biology
  • Transmembrane protein
  • Tryptophan

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