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Identification of tyrosine 189 and asparagine 358 of the cholecystokinin 2 receptor in direct interaction with the crucial C-terminal amide of cholecystokinin by molecular modeling, site-directed mutagenesis, and structure/affinity studies.
Galés C, Poirot M, Taillefer J, Maigret B, Martinez J, Moroder L, Escrieut C, Pradayrol L, Fourmy D, Silvente-Poirot S. Galés C, et al. Among authors: maigret b. Mol Pharmacol. 2003 May;63(5):973-82. doi: 10.1124/mol.63.5.973. Mol Pharmacol. 2003. PMID: 12695525
The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor. Evidence for a crucial role of Met-121 in the activation process.
Escrieut C, Gigoux V, Archer E, Verrier S, Maigret B, Behrendt R, Moroder L, Bignon E, Silvente-Poirot S, Pradayrol L, Fourmy D. Escrieut C, et al. Among authors: maigret b. J Biol Chem. 2002 Mar 1;277(9):7546-55. doi: 10.1074/jbc.M108563200. Epub 2001 Nov 27. J Biol Chem. 2002. PMID: 11724786 Free article.
Identification of putative amino acids of the CCK1R binding site was achieved by dynamics-based docking of the ligand CCK in a refined three-dimensional model of the CCK1R using, as constraints, previous results that identified contact points between residues of CCK and CCK1R (Ke …
Identification of putative amino acids of the CCK1R binding site was achieved by dynamics-based docking of the ligand CCK in a refined three …
144 results