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• W2080679265 abstract "The P2Y14 receptor (P2Y14R) is a Gi protein-coupled receptor that is activated by uracil nucleotides UDP and UDP-glucose. The P2Y14R structure has yet to be solved through X-ray crystallography, but the recent agonist-bound crystal structure of the P2Y12R provides a potentially suitable template for its homology modeling for rational structure-based design of selective and high-affinity ligands. In this study, we applied ligand docking and molecular dynamics refinement to a P2Y14R homology model to qualitatively explain structure–activity relationships of previously published synthetic nucleotide analogues and to probe the quality of P2Y14R homology modeling as a template for structure-based design. The P2Y14R model supports the hypothesis of a conserved binding mode of nucleotides in the three P2Y12-like receptors involving functionally conserved residues. We predict phosphate group interactions with R2536.55, K2777.35, Y2566.58 and Q2606.62, nucleobase (anti-conformation) π–π stacking with Y1023.33 and the role of F1915.42 as a means for selectivity among P2Y12-like receptors. The glucose moiety of UDP-glucose docked in a secondary subpocket at the P2Y14R homology model. Thus, P2Y14R homology modeling may allow detailed prediction of interactions to facilitate the design of high affinity, selective agonists as pharmacological tools to study the P2Y14R." @default.
• W2080679265 created "2016-06-24" @default.
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• W2080679265 date "2015-07-01" @default.
• W2080679265 modified "2023-09-24" @default.
• W2080679265 title "Molecular modeling of the human P2Y14 receptor: A template for structure-based design of selective agonist ligands" @default.
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• W2080679265 doi "https://doi.org/10.1016/j.bmc.2015.03.042" @default.
• W2080679265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4468048" @default.
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