Understanding interactions of gastric inhibitory polypeptide (GIP) with its G-protein coupled receptor through NMR and molecular modeling

Journal of Peptide Science

Volumn 13, Issue 5, 2007, Pages 287-300

  Malde, Alpeshkumar K ^a   Srivastava, Sudha S ^b   Coutinho, Evans C ^a  

^a BOMBAY COLLEGE OF PHARMACY   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

2D NMR; Diabetes; FTDOCK; G protein coupled receptor (GPCR); Gastric inhibitory polypeptide (GIP); GIP receptor (GIPR); GIP(1 30)NH2; Homology modeling; MD simulations

Indexed keywords

CORTICOTROPIN RELEASING FACTOR RECEPTOR; DIMETHYL SULFOXIDE; G PROTEIN COUPLED RECEPTOR; GASTRIC INHIBITORY POLYPEPTIDE; GLUTAMINE; ISOLEUCINE; LYSINE; MEMBRANE PROTEIN; RHODOPSIN; WATER;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; COW; CRYSTAL STRUCTURE; EXTRACELLULAR MATRIX; HUMAN; INTRACELLULAR SPACE; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN STRUCTURE; SIMULATION;

DIABETES MELLITUS, TYPE 2; GASTRIC INHIBITORY POLYPEPTIDE; GASTROINTESTINAL AGENTS; GLUCOSE; HUMANS; INSULIN; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, GASTROINTESTINAL HORMONE; STRUCTURE-ACTIVITY RELATIONSHIP;

BOVINAE;

EID: 34248328787     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.839     Document Type: Article

References (67)

1. Sarabu R, Tilley J. Recent advances in therapeutic approaches to Type 2 Diabetes. Annu. Rep. Med. Chem. 2004; 39: 39-56.
2. Zimmet P, Alberti KG, Shaw J. Global and societal implications of the diabetes epidemic. Nature 2001; 414: 782-787.
3. Zhang B, Moller DE. New approaches in the treatment of type 2 diabetes. Curr. Opin. Chem. Biol. 2000; 4: 461-467.
4. Moller DE. New drug targets for type 2 diabetes and the metabolic syndrome. Nature 2001; 414: 821-827.
5. Kieffer TJ. GIP or not GIP? That is the question. Trends Pharmacol. Sci. 2003; 24: 110-112.
6. Vella A, Rizza RA. New insights into the regulation of glucagon secretion by glucagon-like peptide-1. Horm. Metab. Res. 2004; 36: 822-829.
7. Holz GG, Chepurny OG. Glucagon-like peptide-1 synthetic analogs: new therapeutic agents for use in the treatment of diabetes mellitus. Curr. Med. Chem. 2003; 10: 2471-2483.
8. Irwin N, Green BD, Gault VA, Greer B, Harriott P, Bailey CJ, Flatt PR, O'Harte PM. Degradation, insulin secretion and antihyperglycemic actions of two palmitate-derivitized N-terminal pyroglutamyl analogues of glucose-dependent insulinotropic polypeptide. J. Med. Chem. 2005; 48: 1244-1250.
9. Moody AJ, Thim L, Valverde I. Isolation and sequencing of human gastric inhibitory peptide (GIP). FEBS 1984; 172: 142-148.
10. Brown JC, Dryburgh JR. A gastric inhibitory polypeptide. II. The complete amino acid sequence. Can. J. Biochem. 1971; 49: 867-872.
11. Meier JJ, Nauck MA, Schmidt WE, Gallwitz B. Gastric inhibitory polypeptide: the neglected incretin revisited. Regul. Pept. 2002; 107: 1-13.
12. Meier JJ, Gallwitz B, Nauck MA. Glucagon-Like peptide 1 and gastric inhibitory polypeptide: potential applications in Type 2 diabetes mellitus. BioDrugs 2003; 17: 93-102.
13. Gault VA, Parker JC, Harriott P, Flatt PR, O'Harte FP. Evidence that the major degradation product of glucose-dependent insulinotropic polypeptide, GIP(3-42), is a GIP receptor antagonist in vivo. J. Endocrinol. 2002; 175: 525-533.
14. O'Harte FPM, Gault VA, Parker JC, Harriott P, Mooney MH, Bailey Cd, Flatt PR. Improved stability, insulin-releasing activity and antidiabetic potential of two novel N-terminal analogues of gastric inhibitory polypeptide: N-acetyl-GIP and pGlu-GIP. Diabetologia 2002; 45: 1281-1291.
15. Gault VA, Flatt PR, Bailey Cd, Harriott P, Greer B, Mooney MH, O'Harte FPM. Enhanced cAMP generation and insulin-releasing potency of two novel Tyrl-modified enzyme-resistant forms of glucose-dependent insulinotropic polypeptide is associated with significant antihyperglycaemic activity in spontaneous obesity-diabetes. Biochem. J. 2002; 367: 913-920.
16. Gault VA, Irwin N, Harriott P, Flatt PR, O'Harte FPM. DPP IV resistance and insulin releasing activity of a novel di-substituted analogue of glucose-dependent insulinotropic polypeptide, (Ser2-Asp13)GIP. Cell Biol. Int. 2003; 27: 41-46.
17. Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 2000; 21: 90-113.
18. Harmer AJ. Family-B G-protein-coupled receptors. Genome Biol. 2001; 2: 3013.1-3013.10.
19. Hoare SRJ. Mechanisms of peptide and nonpeptide ligand binding to class B G-protein-coupled receptors. Drug Discov. Today 2005; 10: 417-427.
20. Fehmann HC, Goke B. Characterization of GIP(1-30) and GIP(1-42) as. stimulators of proinsulin gene transcription. Peptides 1995; 16: 1149-1152.
21. Insight-II 2005, Felix 97, Accelrys Inc. San Diego, CA, USA.
22. Sybyl 7.1, Tripos Associates Inc., 1699 S Hanley Rd., St. Louis, MO 631444, USA.
23. Gabb HA, Jackson RM. Sternberg MJE. Modelling protein docking using shape complementarity, electrostatics and biochemical information. J. Mol. Biol. 1997; 272: 106-120.
24. Alana I, Hewage CM, Malthouse JPG, Parker JC, Gault VA. O'Harte FPM. NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide. Biochem. Biophys. Res. Commun. 2004; 325: 281-286.
25. Alana I, Parker JC, Gault VA, Flatt PR, O'Harte FPM, Malthouse JPG, Hewage CM. NMR and alanine scan studies of glucose-dependent insulinotropic polypeptide in water. J. Biol. Chem. 2006; 281: 16370-16376.
26. 7.9]-SP by CD, NMR and MD simulations. Peptides 2005; 26: 875-885.
27. Kanyalkar M, Srivastava S, Coutinho E. Conformation of N-terminal HIV-1 tat (fragment 1-9) peptide by NMR and MD simulations. J. Pept. Sci. 2001; 7: 579-587.
28. Tauro S, Coutinho E, Srivastava S. Conformation of the peptide antibiotic-histatin 8 in aqueous and non aqueous media. Lett. Pept. Sci. 2001; 8: 295-307.
29. Desai P, Coutinho E, Srivastava S, Haq W, Katti SB. Conformation of an immunoreactive undecapeptide fragment (10-20) of Asp φ1 by NMR and molecular modeling. Lett. Pept. Sci. 2002; 9: 21-34.
30. Desai P, Coutinho E, Srivastava S. Conformational diversity of T-kinin in DMSO, water and HFA. Eur. J. Med. Chem. 2002; 37: 135-146.
31. Sklenar V, Piotto M, Leppik K, Saudek V. Gradient-tailored water suppression for 1H-15N HSQCJ experiments optimized to retain full sensitivity. J. Magn. Reson. A 1993; 102: 241-245.
32. Hwang TL, Shaka AJ. Water suppression that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients. J. Magn. Reson. A 1995; 112: 275-279.
33. Bax A, Davis DG. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985; 65: 355-360.
34. Jeener J, Meier BH, Bachman P, Ernst RR. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 1979; 71: 4546-4553.
35. Wagner R, Berger S. Gradient-selected NOESY-a fourfold reduction of the measurement time for the NOESY experiment. J. Magn. Reson. 1996; 123A: 119-121.
36. Derome AE, Williamson MP. Rapid-pulsing artifacts in double quantum filtered COSY. J. Magn. Reson. 1990; 88: 177-185.
37. Kay LE, Keifer P, Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 1992; 114: 10663-10665.
38. Palmer AG III, Cavanagh J, Wright PE, Rance M. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 1991; 93: 151-170.
39. Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assessment of protein secondary structure through NMR spectroscopy. Biochemistry 1992; 31: 1647-1651.
40. Wüthrich K. NMR of Proteins and Nucleic Acids. Wiley: New York, 1986.
41. Vuister GW, Bax A. Quantitative J correlation: a new approach for measuring homonuclear three-bond J (HNHα) coupling constants in 15 N-enriched proteins. J. Am. Chem. Soc. 1993; 115: 7772-7777.
42. Maple J, Dinur U, Hagler AT. Derivation of force fields for molecular mechanics and dynamics from ab initio energy surfaces. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 5350-5354.
43. NMRchitect User Guide, version 2.3. Biosym Technologies, San Diego, 1993.
44. Khedkar SA, Malde AK, Coutinho EC. Modeling human Neurokinin-1 receptor structure using the crystal structure of bovine rhodopsin. Internet Electron. J. Mol. Des. 2005; 4: 329-341.
45. Volz A, Göke R, Lankat-Buttgereit B, Fehmann H, Bode HP, Göke B. Molecular cloning, functional expression, and signal transduction of the GIP-receptor cloned from a human insulinoma. FEBS Lett. 1995; 373: 23-29.
46. Okada T, Fujiyoshi Y, Silow M, Navarro J, Landau EM, Shichida Y. Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography. Proc. Natl. Acad. Sci U.S.A. 2002; 99: 5982-5987.
47. Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acid Res. 1994; 22: 4673-4680.
48. Dayhoff MO, Barker WC, Hunt LT. Establishing homologies in protein sequences. Meth. Enzymol. 1983; 91: 524-544.
49. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acid Res. 1997; 25: 3389-3402.
50. Grace CRR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc. Natl. Acad. Sci. U.S.A. 2004; 101: 12836-12841.
51. Jackson RM, Gabb HA, Sternberg MJE. Rapid refinement of protein interfaces incorporating solvation: application to the docking problem. J. Mol. Biol. 1998; 276: 265-285.
52. Wüthrich K, Billeter M, Braun W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J. Mol. Biol. 1984; 180: 715-740.
53. Khandelwal P, Seth S, Hosur RV. CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical segment from scorpion neurotoxin. Eur. J. Biochem. 1999; 264: 468-478.
54. Chang X, Keller D, Bjorn S, Led JJ. Structure and folding of glucagon-like peptide 1-7-(7-36)-amide in aqueous trifluoroethanol studied by NMR. Magn. Reson. Chem. 2001; 39: 477-483.
55. Andersen NH, Brodsky Y, Neidigh JW, Prickett KS. Medium-dependence of the secondary structure ofexendin-4 and glucagon-like-peptide-1. Bioorg. Med. Chem. 2002; 10: 79-85.
56. Braun W, Wider G, Lee KH. Wüthrich K. Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance. J. Mol. Biol. 1983; 169: 921-948.
57. Manhart S, Hinke SA, McIntosh CH, Pederson RA, Demuth HU. Structure-function analysis of a series of novel GIP analogues containing different helical length linkers. Biochemistry 2003; 42: 3081-3088.
58. Gallwitz B, Witt M, Morys-Wortmann C, Folsch UR, Schmidt WE. GLP-1/GIP chimeric peptides define the structural requirements for specific ligand-receptor interaction of GLP-1. Regul. Pept. 1996; 63: 17-22.
59. Hinke SA, Manhart S, Pamir N, Demuth H, Gelling RW, Pederson RA, McIntosh CHS. Identification of a bioactive domain in the amino-terminus of Glucose-dependent Insulinotropic Polypeptide (GIP). Biochem. Biophys. Acta 2001; 1547: 143-155.
60. Dong M, Li Z, Zang M, Pinon DI, Lybrand TP, Miller LJ. Spatial approximation between two residues in the mid-region of secretin and the amino terminus of its receptor: incorporation of seven sets of such constraints into a three-dimensional model of the agonist-bound secretin receptor. J. Biol. Chem. 2003; 278: 48300-48312.
61. Gensure RC, Carter PH, Petroni BD, Juppner H, Gardella TJ. Identification of determinants of inverse agonism in a constitutively active parathyroid hormone/parathyroid hormone-related peptide receptor by photoaffinity cross-linking and mutational analysis. J. Biol. Chem. 2001; 278: 42692-42699.
62. Dong M, Pinon DI, Cox RF, Miller LJ. Importance of the amino terminus in secretin family G protein-coupled receptors: intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor. J. Biol. Chem. 2004; 279: 1167-1175.
63. Klose JA, Fechner K, Beyermann M, Krause E, Wendt N, Bienert M, Rudolph R, Rothemund S. Impact of N-terminal domains for corticotropin-releasing factor (CRF) receptor-ligand interactions. Biochemistry 2005; 44: 1614-1623.
64. Runge S, Gram C, Brauner-Osborne H, Madsen K, Knudsen LB, Wulff BS. Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus. J. Biol. Chem. 2003; 278: 28005-28010.
65. Gelling RW, Coy DH, Pederson RA, Wheeler MB, Honke S, Kwan T, McIntosh CHS. GIP(6-30amide) contains the high affinity binding region of GIP and is a potent inhibitor of GIP 1-42 action in vitro. Regul. Pept. 1997; 69: 151-154.
66. Gault VA, O'Harte FPM, Harriott P, Flatt PR. Characterization of the cellular and metabolic effects of a novel enzyme-resistant antagonist of glucose-dependent insulinotropic polypeptide. Biophys. Biochem. Res. Commun. 2002; 290: 1420-1426.
67. Perret J, Van Craenenbroeck M, Langer I, Vertongen P, Gregoire F, Robberecht P, Waelbroeck M. Mutational analysis of the glucagon receptor: similarities with the vasoactive intestinal peptide (VIP)/ pituitary adenylate cyclase-activating peptide (PACAP)/secretin receptors for recognition of the ligand's third residue. Biochem. J. 2002; 362: 389-394.