Neuropeptides
Volume 44, Issue 2 , Pages 127-132 , April 2010

VPAC1 receptor binding site: Contribution of photoaffinity labeling approach

References 

  1. Abad C, Martinez C, Juarranz MG, Arranz A, Leceta J, Delgado M, et al. Therapeutic effects of vasoactive intestinal peptide in the trinitrobenzene sulfonic acid mice model of Crohn’s disease. Gastroenterology. 2003;124:961–971
  2. Abad C, Gomariz RP, Waschek JA. Neuropeptide mimetics and antagonists in the treatment of inflammatory disease: focus on VIP and PACAP. Current Topics in Medicinal Chemistry. 2006;6:151–163
  3. Bourgault S, Vaudry D, Ségalas-Milazzo I, Guilhaudis L, Couvineau A, Laburthe M, et al. Molecular and conformational determinants of pituitary adenylate cyclase-activating polypeptide (PACAP) for activation of the PAC1 receptor. Journal of Medicinal Chemistry. 2009;52:3308–3316
  4. Brenneman DE. Neuroprotection: a comparative view of vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide. Peptides. 2007;28:1720–1766
  5. Brubaker PL. Incretin-based therapies: mimetics versus protease inhibitors. Trends in Endocrinology and Metabolism. 2007;18:240–245
  6. Campbell RM, Bongers J, Felix AM. Rational design, synthesis, and biological evaluation of novel growth hormone releasing factor analogues. Biopolymers. 1995;37:67–88
  7. Ceraudo E, Murail S, Tan YV, Lacapère JJ, Neumann JM, Couvineau A, et al. The vasoactive intestinal peptide (VIP) alpha-helix up to C terminus interacts with the N-terminal ectodomain of the human VIP/Pituitary adenylate cyclase-activating peptide 1 receptor: photoaffinity, molecular modeling, and dynamics. Molecular Endocrinology. 2008;22:147–155
  8. Ceraudo E, Tan YV, Nicole P, Couvineau A, Laburthe M. The N-terminal parts of VIP and antagonist PG97–269 physically interact with different regions of the human VPAC1 receptor. Journal of Molecular Neuroscience. 2008;36:245–248
  9. Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science. 2007;318:1258–1265
  10. Christopoulos A, Christopoulos G, Morfis M, Adawela M, Laburthe M, Couvineau A, et al. Novel receptor partners and function of receptor activity-modifying proteins. Journal of Biological Chemistry. 2002;278:3293–3297
  11. Delgado M, Abad C, Martinez C, Leceta J, Gomariz RP. Vasoactive intestinal peptide prevents experimental arthritis by downregulating both autoimmune and inflammatory components of the disease. Nature Medicine. 2001;7:563–568
  12. Delgado M, Pozo D, Ganea D. The significance of vasoactive intestinal peptide in immunomodulation. Pharmacological Reviews. 2004;56:249–290
  13. Dickson L, Finlayson K. VPAC and PAC receptors: from ligands to function. Pharmacology and Therapeutics. 2009;121:294–316
  14. Dong M, Lam PC, Pinon DI, Sexton PM, Abagyan R, Miller LJ. Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding. Molecular Pharmacology. 2008;74:413–422
  15. Epstein S. Is cortical bone hip? What determines cortical bone properties?. Bone. 2007;41:S3–8
  16. Firestein GS. VIP: a very important protein in arthritis. Nature Medicine. 2001;7:537–538
  17. Fredrikson R, Schiöth B. G Protein-coupled receptors in human genome. In:  Rognan D editors. Ligand Design for G Protein-coupled receptors. Weinheim: Wiley-VCH; 2006;p. 1–27vol. 30
  18. Gilligan PJ, Li YW. Corticotropin-releasing factor antagonists: recent advances and exciting prospects for the treatment of human diseases. Current Opinion in Drug Discovery and Development. 2004;7:487–497
  19. Gomariz RP, Martinez C, Abad C, Leceta J, Delgado M. Immunology of VIP: a review and therapeutical perspectives. Current Pharmaceutical Design. 2001;7:89–111
  20. Gourlet P, De Neef P, Cnudde J, Waelbroeck M, Robberecht P. In vitro properties of a high affinity selective antagonist of the VIP1 receptor. Peptides. 1997;18:1555–1560
  21. Gozes I, Divinsky I, Pilzer I, Fridkin M, Brenneman DE, Spier AD. From vasoactive intestinal peptide (VIP) through activity-dependent neuroprotective protein (ADNP) to NAP: a view of neuroprotection and celldivision. Journal of Molecular Neuroscience. 2003;20:315–322
  22. Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, et al. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proceedings of the National Academy of Sciences of the United States of America. 2004;101:12836–12841
  23. Harikumar KG, Morfis MM, Lisenbee CS, Sexton PM, Miller LJ. Constitutive formation of oligomeric complexes between family B G protein-coupled vasoactive intestinal polypeptide and secretin receptors. Molecular Pharmacology. 2006;69:363–373
  24. Harikumar KG, Lam PC, Dong M, Sexton PM, Abagyan R, Miller LJ. Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues. Journal of Biological Chemistry. 2007;282:32834–32843
  25. Hoare SRJ. Mechanism of peptide and nonpeptide ligand binding to class B G-protein-coupled receptors. Drug Discovery Today. 2005;10:417–427
  26. Inzucchi SE, McGuire DK. New drugs for the treatment of diabetes: part II: Incretin-based therapy and beyond. Circulation. 2008;117:574–584
  27. Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY, Lane JR, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science. 2008;322:1211–1217
  28. Jeppesen PB. Glucagon-like peptide-2: update of the recent clinical trials. Gastroenterology. 2006;130:S127–131
  29. Laburthe M, Couvineau A, Tan V. Class II G protein-coupled receptors for VIP and PACAP: structure, models of activation and pharmacology. Peptides. 2007;28:1631–1639
  30. Mulder JE, Kolatkar NS, LeBoff MS. Drug insight: existing and emerging therapies for osteoporosis. Nature Clinical Practice Endocrinology and Metabolism. 2006;2:670–680
  31. Neumann JM, Couvineau A, Murail S, Lacapère JJ, Jamin N, Laburthe M. Class-B GPCR activation: is ligand helix-capping the key?. Trends in Biochemical Sciences. 2008;33:314–319
  32. Nicole P, Lins L, Rouyer-Fessard C, Drouot C, Fulcrand P, Thomas A, et al. Identification of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. Journal of Biological Chemistry. 2000;275:24003–24012
  33. Onoue S, Misaka S, Yamada S. Structure-activity relationship of vasoactive intestinal peptide (VIP): potent agonists and potential clinical applications. Naunyn-Schmiedebergs Archives of Pharmacology. 2008;377:579–590
  34. Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science. 2000;289:739–745
  35. Parthier C, Kleinschmidt M, Neumann P, Rudolph R, Manhart S, Schlenzig D, et al. Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor. Proceedings of the National Academy of Sciences of the United States of America. 2007;104:13942–13947
  36. Parthier C, Reedtz-Runge S, Rudolph R, Stubbs MT. Passing the baton in class B GPCRs: peptide hormone activation via helix induction?. Trends in Biochemical Sciences. 2009;34:303–310
  37. Perrin MH, Grace CR, Digruccio MR, Fischer WH, Maji SK, Cantle JP, et al. Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors. Journal of Biological Chemistry. 2007;282:37529–37536
  38. Pioszak AA, Xu HE. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proceedings of the National Academy of Sciences of the United States of America. 2008;105:5034–5039
  39. Pioszak AA, Parker NR, Suino-Powell K, Xu HE. Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1. Journal of Biological Chemistry. 2008;283:32900–32912
  40. Runge S, Thøgersen H, Madsen K, Lau J, Rudolph R. Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. Journal of Biological Chemistry. 2008;283:11340–11347
  41. Said SI. Vasoactive intestinal polypeptide (VIP): current status. Peptides. 1984;5:143–150
  42. Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe HW, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature. 2008;455:497–502
  43. Solano RM, Langer I, Perret J, Vertongen P, Juarranz MG, Robberecht P, et al. Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction. Journal of Biological Chemistry. 2001;276:1084–1088
  44. Sun C, Song D, Davis-Taber RA, Barrett LW, Scott VE, Richardson PL, et al. Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS. Proceedings of the National Academy of Sciences of the United States of America. 2007;104:7875–7880
  45. Tan YV, Couvineau A, Van Rampelbergh J, Laburthe M. Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the N-terminal ectodomain of the human VPAC1 receptor. Journal of Biological Chemistry. 2003;278:36531–36536
  46. Tan YV, Couvineau A, Laburthe M. Diffuse pharmacophoric domains of vasoactive intestinal peptide (VIP) and further insights into the interaction of VIP with the N-terminal ectodomain of human VPAC1 receptor by photoaffinity labeling with [Bpa6]-VIP. Journal of Biological Chemistry. 2004;279:38889–38894
  47. Tan YV, Couvineau A, Murail S, Ceraudo E, Neumann JM, Lacapère JJ, et al. Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling. Journal of Biological Chemistry. 2006;281:12792–12798
  48. Vaudry D, Falluel-Morel A, Bourgault S, Basille M, Burel D, Wurtz O, et al. Pituitary adenylate cyclase-activating polypeptide and its receptors: 20 years after the discovery. Pharmacological Reviews. 2009;61:283–357
  49. Waelbroeck M, Perret J, Vertongen P, Van Craenenbroeck M, Robberecht P. Identification of secretin, vasoactive intestinal peptide and glucagon binding sites: from chimaeric receptors to point mutations. Biochemical Society Transactions. 2002;30:437–441
  50. Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature. 2008;454:486–491
  51. Yadav M, Goetzl EJ. Vasoactive intestinal peptide-mediated Th17 differentiation: an expanding spectrum of vasoactive intestinal peptide effects in immunity and autoimmunity. Annals of the New York Academy of Sciences. 2008;1144:83–89

PII: S0143-4179(09)00137-1

doi: 10.1016/j.npep.2009.11.008

Neuropeptides
Volume 44, Issue 2 , Pages 127-132 , April 2010

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