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 language | English |
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Pages (from-to) | 243-248 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 384 |
Issue number | 2 |
DOIs | |
Publication status | Published - 26 Jun 2009 |
Externally published | Yes |
Keywords
- Agonist ligand
- Conformational switch
- G protein-coupled receptor
- High-resolution NMR
- Peptide helix
- Proline
- Spectrofluorometry
- Structural biology
- Transmembrane protein
- Tryptophan