Sandbox Reserved 1172: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 29: | Line 29: | ||
=== Endocannabinoid Receptor 1 === | === Endocannabinoid Receptor 1 === | ||
LPA<sub>1</sub> also is closely related to the [http://www.nature.com/ijo/journal/v30/n1s/full/0803272a.html cannabinoid | LPA<sub>1</sub> also is closely related to the first of the [http://www.nature.com/ijo/journal/v30/n1s/full/0803272a.html cannabinoid receptors]. This close relation gives CB<sub>1</sub> ([[Cannabinoid Receptor 1]]) the ability to bind to analogs of LPA and vice versa, which opens the possibility of metabolic crosstalk between the two signaling systems. This connection is made possible through ligand phosphorylation and dephosphorylation <ref name="regpeps">PMID: 26091040</ref>. Specifically, complementary access to the LPA<sub>1</sub> binding pocket can be achieved by phosphorylated CB<sub>1</sub> ligand analogs, while complementary access to the CB<sub>1</sub> binding site requires dephosphorylation of LPA<sub>1</sub> ligand analogs. In both cases, a ligand could serve as a primary [https://en.wikipedia.org/wiki/Selective_receptor_modulator receptor modulator] and a simultaneous [https://en.wikipedia.org/wiki/Prodrug prodrug] for a different receptor <ref name="regpeps">PMID: 26091040</ref>. | ||
<scene name='72/721543/Asp129_and_trp210/2'>Residues Asp129 and Trp210</scene> located within the hydrophobic binding pocket of LPA<sub>1</sub> may share responsibility for the preference for long unsaturated acyl chains. These residues are also interesting in regard to GPCR phylogenic evolution. <ref name="regpeps">PMID: 26091040</ref> Trp210 specifically only occurs in this position in 1% of all class A GPCR receptors and is unique to lysophospholipid and cannabinoid receptors. <ref name = 'Van Durme'>Van Durme, J., Horn, F., Costagliola, S., Vriend, G., and Vassart, G. “GRIS: glycoprotein-hormone receptor information system.” Mol. (2006) Endocrinol. 20, 2247-2255' </ref> | <scene name='72/721543/Asp129_and_trp210/2'>Residues Asp129 and Trp210</scene> located within the hydrophobic binding pocket of LPA<sub>1</sub> may share responsibility for the preference for long unsaturated acyl chains. These residues are also interesting in regard to GPCR phylogenic evolution. <ref name="regpeps">PMID: 26091040</ref> Trp210 specifically only occurs in this position in 1% of all class A GPCR receptors and is unique to lysophospholipid and cannabinoid receptors. <ref name = 'Van Durme'>Van Durme, J., Horn, F., Costagliola, S., Vriend, G., and Vassart, G. “GRIS: glycoprotein-hormone receptor information system.” Mol. (2006) Endocrinol. 20, 2247-2255' </ref> | ||
