ArticleBiochemical and biophysical research communications2009
NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: candidate electrostatic interactions and microdomain formation.
Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Structural Insights into β-arrestin/CB1 Receptor Interaction: NMR and CD Studies on Model Peptides.International journal of molecular sciences · 2020Article
- Molecular Interaction between Distal C-Terminal Domain of the CBJournal of chemical information and modeling · 2019Article
- Article
- Molecular-interaction and signaling profiles of AM3677, a novel covalent agonist selective for the cannabinoid 1 receptor.ACS chemical neuroscience · 2015Article
- Small expression tags enhance bacterial expression of the first three transmembrane segments of the apelin receptor.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2014Article
- Guided reconstitution of membrane protein fragments.Biopolymers · 2014Article
- Structure of the C-terminal region of the Frizzled receptor 1 in detergent micelles.Molecules (Basel, Switzerland) · 2013Article
- Large multiple transmembrane domain fragments of a G protein-coupled receptor: biosynthesis, purification, and biophysical studies.Biopolymers · 2012Article
- The cannabinoid type-1 receptor carboxyl-terminus, more than just a tail.Journal of neurochemistry · 2011Review
- Binding between a distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2.Biochemistry · 2011Article
- Human cannabinoid 1 GPCR C-terminal domain interacts with bilayer phospholipids to modulate the structure of its membrane environment.The AAPS journal · 2011Article
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Authors and funding
6 authors.
Funding
Abstract
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.
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