The mechanism of interaction of sweet proteins with the T1R2-T1R3 receptor: Evidence from the solution structure of G16A-MNEI

Journal of Molecular Biology

Volumn 328, Issue 3, 2003, Pages 683-692

  Spadaccini, Roberta ^a   Trabucco, Franca ^a   Saviano, Gabriella ^b   Picone, Delia ^a   Crescenzi, Orlando ^a   Tancredi, Teodorico ^c   Temussi, Piero A ^a,d  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b UNIVERSITY OF MOLISE   (Italy)

^c CNR   (Italy)

^d NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

Monellin; NMR structure; Structural mutant; Sweet proteins; Taste receptor

Indexed keywords

MONELLIN; MUTANT PROTEIN; PROTEIN; PROTEIN G16A; PROTEIN T1R2; PROTEIN T1R3; SWEET PROTEIN; SWEETENING AGENT; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; MOLECULAR WEIGHT; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TASTE BUD; WILD TYPE;

EID: 0037414437     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00346-2     Document Type: Article

References (59)

1. Kitagawa M., Kusakabe Y., Miura H., Ninomiya Y., Hino A. Molecular genetic identification of a candidate receptor gene for sweet taste. Biochem. Biophys. Res. Commun. 283:2001;236-242.
2. Max M., Shanker Y.G., Huang L., Rong M., Liu Z., Campagne F., et al. Tas1r3, encoding a new candidate taste receptor, is allelic to the sweet responsiveness locus Sac. Nature Genet. 28:2001;58-63.
3. Montmayeur J.P., Liberles S.D., Matsunami H., Buck L.B. A candidate taste receptor gene near a sweet taste locus. Nature Neurosci. 4:2001;492-498.
4. Sainz E., Korley J.N., Battey J.F., Sullivan S.L. Identification of a novel member of the T1R family of putative taste receptors. J. Neurochem. 77:2001;896-903.
5. Nelson G., Hoon M.A., Chandrashekar J., Zhang Y., Ryba N.J.P., Zuker C.S. Mammalian sweet taste receptors. Cell. 106:2001;381-390.
6. Shallenberger R.S., Acree T. Molecular theory of sweet taste. Nature. 216:1967;480-482.
7. Kier L.B. Molecular theory of sweet taste. J. Pharm. Sci. 61:1972;1394-1397.
8. Temussi P.A., Lelj F., Tancredi T. Three-dimensional mapping of the sweet taste receptor site. J. Med. Chem. 21:1978;1154-1158.
9. Temussi P.A., Lelj F., Tancredi T., Castiglione-Morelli M.A., Pastore A. Soft agonist-receptor interactions: theoretical and experimental simulation of the active site of the receptor site of sweet molecules. Int. J. Quantum Chem. 26:1984;889-906.
10. Temussi P.A., Lelj F., Tancredi T. Structure-activity relationship of sweet molecules. Walters D.E., Orthofer F.T., DuBois G.E. Sweeteners, Discovery, Molecular Design and ChemoReception. 450:1991;143-161 ACS Symposium Series 450, ACS, Washington DC.
11. Iwamura H. Structure-sweetness relationship of L-aspartyl dipeptide analogues. A receptor site topology. J. Med. Chem. 24:1981;572-578.
12. Goodman M., Coddington J., Mierke D.F. A model for the sweet taste of stereoisomeric retro-inverso and dipeptide amides. J. Am. Chem. Soc. 109:1987;4712-4714.
13. Moncrieff R.W. The Chemical Senses. 1967;Hill, London.
14. Morris J.A. Sweetening agents from natural sources. Lloydia. 39:1976;25-38.
15. Li X., Staszewski L., Xu H., Durick K., Zoller M., Adler E. Human receptors for sweet and umami taste. Proc. Natl Acad. Sci. USA. 99:2002;4692-4696.
16. Hung L.W., Kohmura M., Ariyoshi Y., Kim S.H. Structural differences in D and L-monellin in the crystals of racemic mixture. J. Mol. Biol. 8:1999;311-321.
17. Caldwell J.E., Abildgaard F., Dzakula Z., Ming D., Hellekant G., Markley J.L. Solution structure of the thermostable sweet-tasting protein brazzein. Nature Struct. Biol. 5:1998;427-431.
18. Ariyoshi Y., Kohmura M. Solid-phase synthesis and structure-activity relationships of analogs of the sweet protein monellin. J. Soc. Synth. Org. Chem. Jpn. 52:1994;359-369.
19. Somoza J.R., Cho J.M., Kim S.H. The taste-active regions of monellin, a potently sweet protein. Chem. Senses. 20:1995;61-68.
20. Temussi P.A. Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor. FEBS Letters. 526:2002;1-3.
21. Spadaccini R., Crescenzi O., Tancredi T., De Casamassimi N., Saviano G., Scognamiglio R., et al. Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin. J. Mol. Biol. 305:2001;505-514.
22. Niccolai N., Spadaccini R., Scarselli M., Bernini A., Crescenzi O., Spiga F., et al. Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe. Protein Sci. 10:2001;1498-1507.
23. Iijima H., Morimoto K. Controlling susceptibility against protease digestion. Ann. N. Y. Acad. Sci. 750:1995;62-65.
24. 15N NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters. 69:1980;185-188.
25. Aue W.P., Bartholdi E., Ernst R.R. Two dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 64:1976;2229-2246.
26. Bax A., Davis D.G. Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
27. Jeener J., Meyer B.H., Bachman P., Ernst R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:1979;4546-4553.
28. Zuiderweg E.R.P., Fesik S.W. Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry. 28:1989;2387-2391.
29. 15N labeled proteins. J. Am. Chem. Soc. 111:1989;1515-1517.
30. Güntert P., Braun W., Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS, and GLOMSA. J. Mol. Biol. 217:1991;517-530.
31. Johnson B.A., Blevins R.A. NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
32. Güntert P., Mumenthaler C., Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:1997;283-298.
33. 15N enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777.
34. 15N with side chain Hβ resonances in larger proteins. J. Magn. Reson. 95:1991;636-641.
35. Griesinger C., Sørensen O.W., Ernst R.R. Two-dimensional correlation of connected transitions. J. Am. Chem. Soc. 107:1986;6394-6396.
36. Pearlman D.A., Case D.A., Caldwell J.W., Ross W.S., Cheatham T.E. III, DeBolt S., Ferguson D., et al. AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comput. Phys. Commun. 91:1995;1-41.
37. 1H NMR investigation of pMNEI. FEBS Letters. 310:1992;27-30.
38. 1H chemical shifts in proteins. J. Biomol. NMR. 9:1997;359-369.
39. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.
40. Ramachandran G.N., Sasisekharan V. Conformation of polypeptides and proteins. Advan. Protein Chem. 23:1968;283-437.
41. Murzin A.G. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors. J. Mol. Biol. 230:1993;689-694.
42. Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T., et al. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature. 407:2000;971-977.
43. 3+. Proc. Natl Acad. Sci. USA. 99:2002;2660-2665.
44. Peitsch M.C. Protein modelling by E-Mail. Bio/Technology. 13:1995;658-660.
45. Peitsch M.C. ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24:1996;274-279.
46. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis. 18:1997;2714-2723.
47. Vakser I.A. Protein docking for low-resolution structures. Protein Eng. 8:1995;371-377.
48. Vakser I.A., Matar O.G., Lam C.F. A systematic study of low-resolution recognition in protein-protein complexes. Proc. Natl Acad. Sci. USA. 96:1999;8477-8482.
49. Margolskee R.F. Molecular mechanisms of bitter and sweet taste transduction. J. Biol. Chem. 277:2002;1-4.
50. Sung Y.H., Shin J., Chang H.J., Cho J.M., Lee W. Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness. J. Biol. Chem. 276:2001;19624-19630.
51. Delaglio F., Grzesiek S., Vuister G., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidimensioal spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;277-293.
52. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR. 6:1995;135-140.
53. Cavanagh J., Rance M. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J. Magn. Reson. 96:1992;670-678.
54. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113:1983;967-971.
55. Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-666.
56. Bax A., Ikura M., Kay L.E., Torchia D.A., Tschudin R. Comparison of different modes of two-dimensional reverse correlation NMR for the study of proteins. J. Magn. Reson. 86:1990;304-318.
57. Weiner S.J., Kollman P.A., Nguyen D.T., Case D.A. An all-atom force-field for simulations of proteins and nucleic acids. J. Comput. Chem. 7:1986;230-238.
58. Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structure. J. Mol. Graph. 14:1996;51-55.
59. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 24:1997;4876-4882.