Vasopressin V2 Receptor/Bioligand Interactions |
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Authors: | Czaplewski Cezary Ka?mierkiewicz Rajmund Ciarkowski Jerzy |
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Institution: | (1) Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, PL-80-952 Gdańsk, Poland |
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Abstract: | Summary We predict some essential interactions between the V2 vasopressin renal receptor (V2R) and its agonists Arg8]vasopressin (AVP) and D-Arg8]vasopressin (DAVP), and the non-peptide antagonist OPC-31260. V2R controls antidiuresis and belongs to the superfamily of
heptahelical transmembrane (7TM) G-protein-coupled receptors (GPCRs). The receptor was built, the ligands were docked and
the structures relaxed using advanced molecular modeling techniques. Docked agonists and antagonists appear to prefer similar
V2R compartments. A number of receptor amino acid residues are indicated, mainly in the TM3-TM7 helices, as potentially important
in ligand binding. Many of these residues are invariant for either the GPCR superfamily or the subfamily of related (vasopressin
V2R, V1aR and V1bR and oxytocin OR) receptors. Moreover, some of the equivalent residues in V1aR have already been found critical
for ligand affinity Mouillac et al., J. Biol. Chem., 270 (1995) 25771]. |
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Keywords: | agonist AMBER 4 1 antagonist constrained simulated annealing GPCR |
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