Molecular Dynamics of a Vasopressin V2 Receptor in a Phospholipid Bilayer Membrane

References

• 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., 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. 1995; 92: 11578–11582
   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
• Baldwin J. M. The probable arrangements of the helices in G protein-coupled receptors. EMBO J. 1993; 12: 1693–1703
   PubMed Web of Science ®Google Scholar
• Herzyk P., Hubbard R. E. Automated method for modeling seven-helix transmembrane receptor from experimental data. Biophys J. 1995; 69: 2419–2442
   PubMed Web of Science ®Google Scholar
• Pebay-Peyroula E., Rummel G., Rosenbusch J. P., Landau E. M. X-ray structure of bacteriorhodopsin at 2.5 angstrom from microcrystals growth in lipid cubic phases. Science 1997; 277: 1676–1681
   PubMed Web of Science ®Google Scholar
• Kimura Y., Vassylyev D. G., Miyazawa A., Kidera A., Matsushima M., Mitsuoka K., Murata K., Hirai T., Fujiyoshi Y. Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature 1997; 389: 206–211
   PubMed Web of Science ®Google Scholar
• Underwood D. J., Strader C. D., Rivero R., Patchett A. A., Greenlee W., Prendergast K. Structural model of the antagoniost and agonist binding to the angiotensin ii, atl subtype, g protein coupled receptor. Chemistry & Biology 1994; 1: 211–221
   PubMedGoogle Scholar
• Underwood D. J., Prendergast K. Getting it together: signal trans-duction in g-protein coupled receptors by association of receptor domains. Chemistry & Biology 1997; 4: 239–248
   PubMedGoogle Scholar
• Wess J. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of g-protein recognision. FASEB J. 1997; 11: 346–354
   PubMed Web of Science ®Google Scholar
• Elling C. E., Thirstup K., Nielsen S. M., Hjorth S. A., Schwartz T. W. Engineering of the metalion sites as distance constraints in structural and functional analysis of 7tm receptors. Folding & Design 1997; 1: 76–80
   Google Scholar
• Farrens D. J., Altenbach C., Yang K., Hubbell W. L., Khorana H. G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 1996; 274: 768–770
   PubMed Web of Science ®Google Scholar
• Trumpp-Kallmeyer S., Hoflack J., Bruinvels A., Hilbert M. Modeling of g-protein-coupled receptors: application to dopamine, adrenaline serotnin, acetylcholine and mammalian opsin receptor. J. Med. Chem. 1992; 35: 3448–3462
   PubMed Web of Science ®Google Scholar
• Oliveira L., Paiva A. C. M., Sander C., Vriend G. A common step for signal transduction in g protein-coupled receptors. tips 1994; 151: 170–172
   Google Scholar
• Scheer A., Fanelli F., Costa T., De Benedetti P. G., Cotecchia S. Constitutive active mutants of the α1ß-adrenergic receptor: role of highly conserved polar amino acids in receptor activation. EMBO J. 1996; 15: 3566–3578
   PubMed Web of Science ®Google Scholar
• Fanelli F., Menziani M. C., De Benedetti P. G. Computer simulation of signal transduction mechanism in α1β-adrenergic and m3-muscarinic receptors. Protein Eng. 1995; 8: 557–564
   PubMedGoogle Scholar
• Czaplewski C., Kazmierkiewicz R., Ciarkowski J. Molecular modeling of the human vasopressin v2 receptor/agonist complex. J. Comp. Aided Molec. Design 1998; 12: 1–13
   PubMed Web of Science ®Google Scholar
• http://expasy.heugech/swissmod/SWISSS-MODEL.html, Swiss-Model. an automated knowledge-based protein moldeling server at glaxo wellcome research and development s.a. in geneva
   Google Scholar
• v. 6.1 SYBYL. Tripos inc., St Louis, MOUSA 1994
   Google Scholar
• Postina R., Kojro E., Fahrenholz F. Separate agonist and peptide atagonist binding sites of the oxytocin receptor defined by their transfer into v2 vasopressin receptor. J. Biol. Chem. 1996; 271: 31593–31601
   PubMed Web of Science ®Google Scholar
• Schulein R., Liebenoff U., Mnller H., Birnbanmer M., Rosental W. Propeties of the human arginine vasopressin v2 receptor afted site-directed mutagenesis of its putative palmioylation site. Biochem. J. 1996; 313: 611–616
   PubMed Web of Science ®Google Scholar
• Sadeghi H., Innamorati G., Dagarag M., Birnbaumer M. Palmitoylation of the v2 vasopressin receptor. Mol. Pharmacol. 1997; 52: 21–29
   PubMed Web of Science ®Google Scholar
• Pasenkiewicz-Gierula M., Takaoka Y., Miyagawa H., Kitamura K., Kusumi A. Hydrogen bonding of water phosphatidylcholine in the membrane as studied by a molecular dynamics simulation: location, geometry and lipid-lipid bridging via hydrogen-bonded water. J. Phys. Chem. A 1997; 101: 3677–3691
   Web of Science ®Google Scholar
• Pearlman D. A., Case D. A., Caldwell J. W., Ross W. S., Cheathem T. E., III, Ferguson D. M., Seibel G. L., Sigh U. C., Weiner P. K., Kollman P. A. Amber 4.1. Uniwerity of California, San Francisco, CAUSA 1995
   Google Scholar
• Jorgensen W. L., Tirado-Rives J. The OPLS potential function for proteins. energy minimization for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 1988; 110: 1657–1666
   PubMed Web of Science ®Google Scholar
• Jorgensen W. L., Chandrasekhar J., Madura J. D., Impey R., Klein M. L. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 1983; 79: 926–935
   Web of Science ®Google Scholar
• Brooks C. L., III, Karplus M., Pettitt B. M. Proteins: a theoretical perspective of dynamics, structure and termodynamics. Ade. Chem. Phys. 1988; 71: 53
   Google Scholar
• Garmer D. R. Md simulation of a 5-HT24 receptor model in dope membranes. J. Biomol. Struct. & Dynam. 1997; 14: 525–546
   PubMed Web of Science ®Google Scholar
• Barlow D. J., Thorton J. M. Helix geometry in proteins. J. Mol. Biol. 1988; 201: 601–619
   PubMed Web of Science ®Google Scholar
• Mouillac B., Chini B., Balestre M., Elands J., Trumpp-Kallmeyer S., Hoflack J., Hilbert M., Ard S., Barberis C. The binding site of neuropeptide vasopressin via receptor. J. Biol. Chem. 1995; 270: 25771–25777
   PubMed Web of Science ®Google Scholar