Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1933279 | Biochemical and Biophysical Research Communications | 2009 | 6 Pages |
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.
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Authors
Elvis K. Tiburu, Sergiy Tyukhtenko, Lalit Deshmukh, Olga Vinogradova, David R. Janero, Alexandros Makriyannis,