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Publication Abstract from PubMed
We report the NMR solution structure of a synthetic 40-mer (T(377)-E(416)) that encompasses human cannabinoid receptor-1 (hCB1) transmembrane helix 7 (TMH7) and helix 8 (H8) [hCB1(TMH7/H8)] in 30% trifluoroethanol/H(2)O. Structural features include, from the peptide's amino terminus, a hydrophobic alpha-helix (TMH7); a loop-like, 11 residue segment featuring a pronounced Pro-kink within the conserved NPxxY motif; a short amphipathic alpha-helix (H8) orthogonal to TMH7 with cationic and hydrophobic amino-acid clusters; and an unstructured C-terminal end. The hCB1(TMH7/H8) NMR solution structure suggests multiple electrostatic amino-acid interactions, including an intrahelical H8 salt bridge and a hydrogen-bond network involving the peptide's loop-like region. Potential cation-pi and cation-phenolic OH interactions between Y(397) in the TMH7 NPxxY motif and R(405) in H8 are identified as candidate structural forces promoting interhelical microdomain formation. This microdomain may function as a flexible molecular hinge during ligand-induced hCB1 conformer transitions.
NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: candidate electrostatic interactions and microdomain formation.,Tyukhtenko S, Tiburu EK, Deshmukh L, Vinogradova O, Janero DR, Makriyannis A Biochem Biophys Res Commun. 2009 Dec 18;390(3):441-6. Epub 2009 Sep 18. PMID:19766594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Tyukhtenko S, Tiburu EK, Deshmukh L, Vinogradova O, Janero DR, Makriyannis A. NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: candidate electrostatic interactions and microdomain formation. Biochem Biophys Res Commun. 2009 Dec 18;390(3):441-6. Epub 2009 Sep 18. PMID:19766594 doi:10.1016/j.bbrc.2009.09.053
