471 research outputs found
Correction: Howlett et al. The Spicy Story of Cannabimimetic Indoles. <i>Molecules</i> 2021, <i>26</i>, 6190
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Molecular Interaction between Distal C‑Terminal Domain of the CB<sub>1</sub> Cannabinoid Receptor and Cannabinoid Receptor Interacting Proteins (CRIP1a/CRIP1b)
No full textWe have investigated the structure of the distal C-terminal
domain
of the of the CB1 cannabinoid receptor (CB1R) to study
its interactions with CRIP1a and CRIP1b using computational techniques.
The amino acid sequence from the distal C-terminal domain of CB1R
(G417-L472) was found to be unique, as it does
not share sequence similarity with other protein structures, so the
structure was predicted using ab initio modeling.
The computed model of the distal C-terminal region of CB1R has a helical
region between positions 441 and 455. The CRIP1a and CRIP1b were modeled
using Rho-GDI 2 as a template. The three-dimensional model of the
distal C-terminal domain of the CB1R was docked with both CRIP1a as
well as CRIP1b to study the crucial interactions between CB1R and
CRIP1a/b. The last nine residues of CB1R (S464TDTSAEAL4722) are known to be a CRIP1a/b binding site. The majority
of the key interactions were identified in this region, but notable
interactions were also observed beyond theses nine residues. The multiple
interactions between Thr418 (CB1R) and Asn61 (CRIP1a) as well as Asp430
(CB1R) and Lys76 (CRIP1a) indicate their importance in the CB1R–CRIP1a
interaction. In the case of CRIP1b, multiple hydrogen bond interactions
between Asn437 (CB1R) and Glu77 (CRIP1b) were observed. These interactions
can be critical for CB1R’s interaction with CRIP1a/b, and targeting
them for further experimental studies can advance information about
CRIP1a/b functionality
Cannabinoid CB1 receptors transactivate multiple receptor tyrosine kinases and regulate serine/threonine kinases to activate ERK in neuronal cells
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