DOCKING LIGANDS TO VASOPRESSIN AND OXYTOCIN RECEPTORS VIA GENETIC ALGORITHM

REFERENCES

• Vriend G., Horn F. GPCR DataBase 2001©, (http://www.gpcr.org/7tm) (accessed Sept 2001)
   Google Scholar
• Wess J. Structure–Function Analysis of G Protein-Coupled Receptors, J. Wess. Wiley-Liss, Inc. 1999
   Google Scholar
• Leurs R., Smit M. J., Alewijnse A. E., Timmerman H. Agonist-Independent Regulation of Constitutively Active G-Protein-Coupled Receptors. Trends Biochem. Sci. 1998; 23: 418–422
   PubMed Web of Science ®Google Scholar
• Gudermann T., Nuernberg B., Schultz G. Receptors and G Proteins as Primary Components of Transmembrane Signal Transduction. Part 1. G Protein-Coupled Receptors: Structure and Functions. Clin. Invest. 1995; 73: 51–63
   Google Scholar
• Okada T., Le Trong I., Fox B. A., Behnke C. A., Stenkamp R. E., Palczewski K. X-Ray Diffraction Analysis of Three-Dimensional Crystals of Bovine Rhodopsin Obtained from Mixed Micelles. J. Struct. Biol. 2000; 130: 73–80
   PubMed Web of Science ®Google Scholar
• Mouillac B., Chini B., Balestre M.-N., Elands J., Trumpp-Kallmeyer S., Hoflack J., Hibert J., Hibert M., Jard S., Barberis C. The Binding Site of Neuropeptide Vasopressin V1a Receptor. J. Biol. Chem. 1995; 270: 25771–25777
   PubMed Web of Science ®Google Scholar
• Sugimoto T., Saito M., Mochizuki S., Watanabe Y., Hashimoto S., Kawashima H. Molecular Cloning and Functional Expression of a cDNA Encoding the Human V1b Vasopressin Receptor. J. Biol. Chem. 1994; 269: 27088–27092
   PubMed Web of Science ®Google Scholar
• De Keyzer Y., Auzan C., Lenne F., Beldjord C., Thibonnier M., Bertanga X., Clauser E. Cloning and Characterization of the Human V3 Pituitary Vasopressin Receptor. FEBS Lett. 1994; 356: 215–220
   PubMed Web of Science ®Google Scholar
• Kojro E., Eich P., Gimpl G., Fahrenholz F. Direct Identification of an Extracellular Agonist Binding Site in the Renal V2 Vasopressin Receptor. Biochemistry 1993; 32: 13537–13544
   PubMed Web of Science ®Google Scholar
• Willams P. D., Bock M. G., Tung R. D., Garsky V. M., Perlow D. S., Erb J. M., Lundell G. F., Gould N. P., Whitter W. L., Hoffman J. B., Kauffman M. J., Clineschmidt B. V., Pettibone D. J., Freidinger R. M., Veber D. F. Development of a Novel Class of Cyclic Hexapeptide Oxytocin Antagonists Based on a Natural Product. J. Med. Chem. 1992; 35: 3905–3918
   PubMed Web of Science ®Google Scholar
• Palczewski K., Kumasaka T., Hori Y., Behnke C. A., Motoshima H., Fox B. A., Le Trong I., Teller D. C., Okada T., Stenkamp R. E., Yamamoto M., Miyano M. Crystal Structure of Rhodopsin: a G Protein-Coupled Receptor. Science 2000; 289: 739–745
   PubMed Web of Science ®Google Scholar
• Schertler G.F. X., Villa C., Henderson R. Projection Structure of Rhodopsin. Nature 1993; 362: 770–772
   PubMed Web of Science ®Google Scholar
• Unger V. M., Hargrave P. A., Baldwin J. M., Schertler G.F. X. Arrangement of Rhodopsin Transmembrane α-Helices. Nature 1997; 389: 203–206
   PubMed Web of Science ®Google Scholar
• Unger V. M., Schertler G.F. X. Low Resolution Structure of Bovine Rhodopsin Determined by Electron Cryo-Microscopy. Biophys. J. 1995; 68: 1776–1786
   PubMed Web of Science ®Google Scholar
• Schertler G.F. X., Hargrave P. A. Projection Structure of Frog Rhodopsin in Two Crystal Forms. Proc. Natl. Acad. Sci. USA 1995; 92: 11578–11582
   PubMed Web of Science ®Google Scholar
• Baldwin J. M., Schertler G.F. X., Unger V. M. An Alpha-Carbon Template for the Transmembrane Helices in the Rhodopsin Family of G-Protein-Coupled Receptors. J. Mol. Biol. 1997; 272: 144–164
   PubMed Web of Science ®Google Scholar
• Pogozheva I. D., Lomize A. L., Mosberg H. I. The Transmembrane 7-α-Bundle of Rhodopsin: Distance Geometry Calculations with Hydrogen Bonding Constraints. Biophys. J. 1997; 70: 1963–1985
   Google Scholar
• Pogozheva I. D., Lomize A. L., Mosberg H. I. Opioid Receptor Three-Dimensional Structures from Distance Geometry Calculations with Hydrogen Bonding Constraints. Biophys. J. 1998; 75: 612–634
   PubMed Web of Science ®Google Scholar
• Herzyk P., Hubbard R. E. Automated Method for Modeling Seven-Helix Transmembrane Receptors from Experimental Data. Biophys. J. 1995; 69: 2419–2442
   PubMed Web of Science ®Google Scholar
• Herzyk P., Hubbard R. E. Combined Biophysical and Biochemical Information Confirms Arrangement of Transmembrane Helices Visible from the Three-Dimensional Map of Frog Rhodopsin. J. Mol. Biol. 1998; 281: 741–754
   PubMed Web of Science ®Google Scholar
• Ciarkowski J., Drabik P., Gieldon A., Kazmierkiewicz R., Slusarz R. Signal Transmission Via G Protein-Coupled Receptors in View of the Rhodopsin Structure Determination. Acta Biochim. Polonica 2001; 48: 1203–1207
   PubMed Web of Science ®Google Scholar
• SYBYL 6.1. Tripos Inc., USA 1994, 1699 S.Hanley Rd., St. Louis, MO 63144
   Google Scholar
• Gieldon A., Kazmierkiewicz R., Slusarz R., Ciarkowski J. Molecular Modeling of Interactions of the Non-Peptide Antagonist YM087 with the Human Vasopressin V1a V2 Receptors and with Oxytocin Receptors. J. Comp.-Aided Mol. Design 2001; 15: 1085–1104
   PubMed Web of Science ®Google Scholar
• Czaplewski C., Kazmierkiewicz R., Ciarkowski J. Molecular Modeling of the Human Vasopressin V2 Receptor/Agonist Complex. J. Comp.-Aided Mol. Design 1998; 12: 275–287
   PubMed Web of Science ®Google Scholar
• Case D. A., Pearlman D. A., Caldwell J. W., Cheatham III T. E., Ross W. S., Simmerling C., Darden T., Merz K. M., Stanton R. V., Cheng A., Vincent J. J., Crowley M., Ferguson D. M., Radmer R., Seibel G. L., Singh U. C., Wiener P., Kollman P. A. Amber 5.0. University of California, San Francisco 1997
   Google Scholar
• Cornell W. D., Cieplak P., Bayly C. I., Gould I. R., Merz K. M., Jr., Ferguson D. M., Spellmeyer D. C., Fox T., Caldwell J. W., Kollman P. A. A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids and Organic Molecules. J. Am. Chem. Soc. 1995; 117: 5179–5197
   Web of Science ®Google Scholar
• Schmidt M. W., Baldridge K. K., Boatz J. A., Elbert S. T., Gordon M. S., Jensen J. J., Koseki S., Matsunaga N., Nguyen K. A., Su S., Windus T. L., Dupuis M., Montgomery J. A. General Atomic and Molecular Electronic Structure System. J. Comput. Chem. 1993; 14: 1347–1363
   Web of Science ®Google Scholar
• Morris G. M., Goodsell D. S., Halliday R. S., Huey R., Hart W. E., Belew R. K., Olson A. J. Automated Docking Using a Lamarckian Genetic Algorithm and Empirical Binding Free Energy Function. J. Comput. Chem. 1998; 19: 1639–1662
   Web of Science ®Google Scholar
• Solis F. J., Wets R. J.-B. Minimization by Random Search Techniques. Math. Operations Res. 1981; 6: 19–30
   Web of Science ®Google Scholar
• Hockney R. W. The Potential Calculation and Some Applications. Meth. Comp. Phys. 1970; 9: 136–211
   Google Scholar
• Verlet L. Computer Experiments on Classical Fluids. I. Thermodynamical Properties of Lennard-Jones Molecules. Phys. Rev. 1967; 159: 98–103
   Google Scholar
• Gether U., Kobilka B. K. G Protein-Coupled Receptors. Mechanism of Agonist Activation. J. Biol. Chem. 1998; 273: 17979–17982
   PubMed Web of Science ®Google Scholar
• Colson A.-O., Perlman J. H., Smolyar A., Gershengorn M. C., Osman R. Static and Dynamic Roles of Extracellular Loops in G-Protein-Coupled Receptors: A Mechanism for Sequential Binding of Thyrotropin-Releasing Hormone to its Receptor. Biophys. J. 1998; 74: 1087–1100
   PubMed Web of Science ®Google Scholar
• Postina R., Kojro E., Fahrenholz F. Separate Agonist and Peptide Antagonist Binding Sites of the Oxytocin Receptor Defined by Their Tranfer into the V2 Vasopressin Receptor. J. Biol. Chem. 1996; 271: 31593–31601
   PubMed Web of Science ®Google Scholar
• Postina R., Kojro E., Fahrenholz F. Identification of Neurohypophysial Hormone Receptor Domains Involved in Ligand Binding and G Protein Coupling. Adv. Exp. Med. Biol. 1998; 449: 371–385
   PubMed Web of Science ®Google Scholar
• Ufer E., Postina R., Gorbulev V., Fahrenholz F. An Extracellular Residue Determines the Agonist Specificity of V2 Vasopressin Receptors. FEBS Lett. 1995; 362: 19–23
   PubMed Web of Science ®Google Scholar
• Chini B., Mouillac B., Ala Y., Balestre M. N., Trumpp-Kallmeyer S., Hoflack J., Elands J., Hibert M., Manning M., Jard S., Barberis C. Tyr 115 is the Key Residue for Determining Agonist Selectivity in the V1a Vasopressin Receptor. EMBO J. 1995; 14: 2176–2182
   PubMed Web of Science ®Google Scholar
• Hibert M., Hoflack J., Trumpp-Kallmeyer S., Mouillac B., Chini B., Mahe E., Cotte N., Jard S., Manning M., Barberis C. Functional Architecture of Vasopressin/Oxytocin Receptors. J. Recept. Signal Transduct. Res. 1999; 19: 589–596
   PubMed Web of Science ®Google Scholar
• Chini B., Mouillac B., Balestre M.-N., Trumpp-Kallmeyer S., Hoflack J., Hibert M., Andriolo M., Pupier S., Jard S., Barberis C. Two Aromatic Residues Regulate the Response of the Human Oxytocin Receptor to the Partial Agonis Arginine Vasopressin. FEBS Lett. 1996; 397: 201–206
   PubMed Web of Science ®Google Scholar
• Suryanarayana S., Daunt D. A., von Zastrow M., Kobilka B. K. A Point Mutation in the Seventh Hydrophobic Domain of the Alpha 2 Adrenergic Receptor Increases its Affinity for a Family of Beta Receptor Antagonists. J. Biol. Chem. 1991; 266: 15488–15492
   PubMed Web of Science ®Google Scholar
• Metcalf M. A., McGuffin R. W., Hamblin M. W. Conversion of the Human 5-HT1D Beta Serotonin Receptor to the Rat 5-HT1b Ligand-Binding Phenotype by Thr355Asn Site Directed Mutagenesis. Biochem. Pharmacol. 1992; 44: 1917–1920
   PubMed Web of Science ®Google Scholar