scholarly journals Molecular Interaction between Distal C-Terminal Domain of the CB1 Cannabinoid Receptor and Cannabinoid Receptor Interacting Proteins (CRIP1a/CRIP1b)

2019 ◽  
Vol 59 (12) ◽  
pp. 5294-5303
Author(s):  
Pratishtha Singh ◽  
Anjali Ganjiwale ◽  
Allyn C. Howlett ◽  
Sudha M. Cowsik
Keyword(s):  
Molecular Interaction ◽  
Cannabinoid Receptor ◽  
Interacting Proteins ◽  
Terminal Domain ◽  
Cb1 Cannabinoid Receptor ◽  
Receptor Interacting Proteins

scholarly journals Allosteric Modulation of the CB1 Cannabinoid Receptor by Cannabidiol—A Molecular Modeling Study of the N-Terminal Domain and the Allosteric-Orthosteric Coupling

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2456
Author(s):  
Jakub Jakowiecki ◽  
Renata Abel ◽  
Urszula Orzeł ◽  
Paweł Pasznik ◽  
Robert Preissner ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Cannabinoid Receptor ◽  
Binding Mode ◽  
Ligand Docking ◽  
Coupling Mechanism ◽  
Interaction Patterns ◽  
Allosteric Site ◽  
Terminal Domain ◽  
Cb1 Cannabinoid Receptor ◽  
N Terminus

The CB1 cannabinoid receptor (CB1R) contains one of the longest N termini among class A G protein-coupled receptors. Mutagenesis studies suggest that the allosteric binding site of cannabidiol (CBD) involves residues from the N terminal domain. In order to study the allosteric binding of CBD to CB1R we modeled the whole N-terminus of this receptor using the replica exchange molecular dynamics with solute tempering (REST2) approach. Then, the obtained structures of CB1R with the N terminus were used for ligand docking. A natural cannabinoid receptor agonist, Δ9-THC, was docked to the orthosteric site and a negative allosteric modulator, CBD, to the allosteric site positioned between extracellular ends of helices TM1 and TM2. The molecular dynamics simulations were then performed for CB1R with ligands: (i) CBD together with THC, and (ii) THC-only. Analyses of the differences in the residue-residue interaction patterns between those two cases allowed us to elucidate the allosteric network responsible for the modulation of the CB1R by CBD. In addition, we identified the changes in the orthosteric binding mode of Δ9-THC, as well as the changes in its binding energy, caused by the CBD allosteric binding. We have also found that the presence of a complete N-terminal domain is essential for a stable binding of CBD in the allosteric site of CB1R as well as for the allosteric-orthosteric coupling mechanism.

Falcarinol (Panaxynol) is a CB1 cannabinoid receptor antagonist and induces pro-allergic effects in skin

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
J Gertsch ◽  
M Leonti ◽  
L Casu ◽  
F Cottiglia ◽  
S Raduner ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Cannabinoid Receptor ◽  
Cb1 Cannabinoid Receptor

scholarly journals The CB1 cannabinoid receptor mediates excitotoxicity-induced neural progenitor proliferation and neurogenesis. VOLUME 282 (2007) PAGES 23892-23898

2008 ◽  
Vol 283 (9) ◽  
pp. 5971
Author(s):  
Tania Aguado ◽  
Eva Romero ◽  
Krisztina Monory ◽  
Javier Palazuelos ◽  
Michael Sendtner ◽  
...  
Keyword(s):  
Cannabinoid Receptor ◽  
Neural Progenitor ◽  
Cb1 Cannabinoid Receptor

Design, synthesis and biological evaluation of piperazine analogues as CB1 cannabinoid receptor ligands

2008 ◽  
Vol 16 (7) ◽  
pp. 4035-4051 ◽  
Author(s):  
Kwang-Seop Song ◽  
Sung-Han Lee ◽  
Hyun Ji Chun ◽  
Jong Yup Kim ◽  
Myung Eun Jung ◽  
...  
Keyword(s):  
Cannabinoid Receptor ◽  
Biological Evaluation ◽  
Receptor Ligands ◽  
Design Synthesis ◽  
Cb1 Cannabinoid Receptor ◽  
Synthesis And Biological Evaluation
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