Role of aromatic amino acids in carbohydrate binding of plant lectins: Laser photo chemically induced dynamic nuclear polarization study of hevein domain-containing lectins

Proteins: Structure, Function and Genetics

Volumn 28, Issue 2, 1997, Pages 268-284

  Siebert, Hans Christian ^a,b   Von Der Lieth, Claus Wilhelm ^c   Kaptein, Robert ^b   Beintema, Jaap J ^d   Dijkstra, Klaas ^d   Van Nuland, Nico ^d   Soedjanaatmadja, Ukun M S ^e   Rice, Ann ^f   Vliegenthart, Johannes F G ^b   Wright, Christine S ^f   Gabius, Hans Joachim ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b UTRECHT UNIVERSITY   (Netherlands)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^d UNIVERSITY OF GRONINGEN   (Netherlands)

^e PADJADJARAN UNIVERSITY   (Indonesia)

^f VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Agglutinins; Chemically induced dynamic nuclear polarization (CIDNP); Lectins; Molecular modeling; Nuclear magnetic resonance (NMR)

Indexed keywords

AROMATIC AMINO ACID; CARBOHYDRATE BINDING PROTEIN; DYE; HISTIDINE; INDOLE; N ACETYLGLUCOSAMINE; PLANT LECTIN; RADICAL; TRYPTOPHAN; TYROSINE; URTICA DIOICA EXTRACT; WHEAT GERM AGGLUTININ;

ARTICLE; CONFORMATIONAL TRANSITION; LASER; LECTIN BINDING; LIGAND BINDING; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PHOTOCHEMISTRY; POLARIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; ANTIMICROBIAL CATIONIC PEPTIDES; CARBOHYDRATE METABOLISM; LECTINS; MAGNETIC RESONANCE SPECTROSCOPY; PLANT LECTINS; PLANT PROTEINS; PLANTS; PROTEIN BINDING; PROTEIN CONFORMATION;

TRITICUM AESTIVUM; URTICA DIOICA;

EID: 0031007590     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<268::AID-PROT14>3.0.CO;2-G     Document Type: Article

References (66)

1. Sharon, N., Lis, H. Lectins as cell recognition molecules. Science 246:227-234, 1989.
2. Gabius, H.-J. Detection and functions of mammalian lectins: With emphasis on membrane lectins. Biochim. Biophys. Acta 1071:1-18, 1991.
3. Gabius, H.-J., Gabius, S. (eds.) "Lectins and Glycobiology." New York: Springer-Verlag, 1993.
4. Gabius, H.-J., Gabius, S. (eds.) "Glycosciences: Status and Perspectives." Weinheim: Chapman & Hall, 1997.
5. Kaptein, R., Dijkstra, K., Nicolay, K. Laser photo-CIDNP as a surface probe for proteins in solution. Nature 274:293-294, 1978.
6. Kaptein, R. Photo CIDNP studies of proteins. In: "Biological Magnetic Resonance," Vol. 4. Berliner, L. J. (ed.). New York: Plenum, 1982:145-191.
7. Hore, P.J., Broadhurst, R.W. Photo-CIDNP of biopolymers. Prog. NMR Spectrosc. 25:345-402,1993.
8. 2-terminal DNA-binding domain of lac repressor with poly [d(AT)]. Proc. Natl. Acad. Sci. U.S.A. 77:1545-1548, 1980.
9. Stob, S., Scheek, R. M., Boelens, R., Kaptein, R. Photo-CIDNP study of the interaction between lac repressor headpiece and lac operator DNA. FEBS Lett. 239:99-104, 1988.
10. Broadhurst, R.W., Dobson, C.M., Hore, P.J., Radford, S.E., Rees, M.L. A photochemically induced dynamic nuclear polarization study of denaturated states of lysozyme. Biochemistry 30:405-412, 1991.
11. Hård, K., Kamerling, J.P., Vliegenthart, J.F.G. Application of laser photo-CIDNP for an intact glycoprotein in solution. Carbohydr. Res. 236:321-326, 1992.
12. Siebert, H.-C., André, S., Reuter, G., Gabius, H.-J., Kaptein, R., Vliegenthart, J.F.G. Effect of enzymatic desialylation of human serum amyloid P component on surface exposure of laser photo CIDNP (chemically induced dynamic nuclear polarization)-reactive histidine, tryptophan and tyrosine residues. FEBS Lett. 371:13-16, 1995.
13. Wright, C.S. Structural comparison of the two distinct sugar-binding sites in wheat germ agglutinin isolectin II. J. Mol. Biol. 178:91-104, 1984.
14. Wright, C.S. Crystal structure of a wheat germ agglutinin/ glycophorin-sialoglycopeptide receptor complex. J. Biol. Chem. 267:14345-14352, 1992.
15. Quiocho, F. Protein-carbohydrate interactions: Basic molecular features. Pure Appl. Chem. 61:1293-1306, 1989.
16. Imberty, A., Bourne, Y., Cambillau, C., Rouge, P., Perez, S. Oligosaccharide conformation in protein/carbohydrate complexes. Adv. Biophys. Chem. 3:71-117, 1993.
17. Gabius, H.-J. Animal lectins. Eur. J. Biochem., 243:543-576, 1997.
18. 1H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J. Mol. Biol. 258:322-333, 1996.
19. Soedjanaatmadja, U.K.S., Hofsteenge, J., Jeronimus-Stratingh, C.M., Bruins, A.P. Beintema, J.J. Demonstration by mass spectrometry that pseudo-hevein and hevein have ragged C-terminal sequences. Biochim. Biophys. Acta 1209:144-148, 1994.
20. Soedjanaatmadja, U.K.S., Subroto, T., Beintema, J.J. The effluent of natural rubber factories is enriched in the antifungal protein hevein. Bioresource Technol. 53:39-41, 1995.
21. Chrispeels, M.J., Raikhel, N.V. Lectins, lectin genes, and their role in plant defence. Plant Cell 3:1-9, 1991.
22. Gidrol, X., Chrestin, H., Tan, H.-L., Kush, A. Hevein, a lectin-like protein from Hevea brasiliensis (rubber tree), is involved in coagulation of latex. J. Biol. Chem. 269:9278-9283, 1994.
23. Peumans, W.J., van Damme, E.J.M. Lectins as plant defence proteins. Plant Physiol. 109:347-352, 1995.
24. Rüdiger, H. Structure and function of plant lectins. In: "Glycosciences: Status and Perspectives." Gabius, H.-J., Gabius, S. (eds.) Weinheim: Chapman & Hall, 1997:415-438.
25. Shibuya, N., Goldstein, I.J., Schafer, J.A., Peumans, W.J., Broeckaert, W.F. Carbohydrate binding properties of the stinging nettle (Urtica dioica) rhizome lectin. Arch. Biochem. Biophys. 249:215-224, 1986.
26. Beintema, J.J., Peumans, W.J. The primary structure of stinging nettle (Urtica dioica) agglutinin. FEBS Lett. 299:131-134, 1992.
27. Galelli, A., Truffa-Bachi, P. Urtica dioica agglutinin: A superantigenic lectin from stinging nettle rhizome. J. Immunol. 151:1821-1831, 1993.
28. Gabius, H.-J. Lectinology meets mythology: Oncological future for the mistletoe lectin? Trends Glycosci. Glycotechnol. 6:229-238, 1994.
29. Gabius, H.-J., Gabius, S., Joshi, S.S., Koch, B., Schroeder, M., Manzke, W. M., Westerhausen, M. From ill-defined extracts to the immunomodulatory lectin: Will there be a reason for oncological application of mistletoe? Planta Med. 60:2-7, 1994.
30. Gabius, H.-J., Kayser, K., Gabius, S. Protein-Zucker-Erkennung. Grundlagen und medizinische Anwendungen am Beispiel der Tumorlektinologie. Naturwissenschaften 82:533-543, 1995.
31. Wright, H.T., Brooks, D.M., Wright, C.S. Evolution of the multidomain protein wheat germ agglutinin. J. Mol. Evol. 21:133-138, 1985.
32. Wright, C.S., Raikhel, N. Sequence variability in three wheat germ agglutinin isolectins: Products of multiple genes in polyploid wheat. J. Mol. Evol. 28:327-336, 1989.
33. Wright, H.T., Sandrasegaram, G., Wright, C.S. Evolution of a family of N-acetylglucosamine-binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J. Mol. Evol. 33:283-294, 1991.
34. Wright, C.S. Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 Å resolution. J. Mol. Biol. 194:501-529, 1987.
35. Wright, C.S. Comparison of the refined crystal structure of two wheat germ agglutinin isolectins. J. Mol. Biol. 209:475-487, 1989.
36. Wright, C.S. 2.2 Å resolution structure analysis of two refined N-acetylneuraminyllactose-wheat germ agglutinin isolectin complexes. J. Mol. Biol. 215:635-651, 1990.
37. Wright, C.S., Jaeger, J. Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A. J. Mol. Biol. 232:620-638, 1993.
38. Rice, A.C. "Cloning, Expression, Purification and Characterization of Domain B of Wheat Germ Agglutinin." Doctoral thesis, Virginia Commonwealth University, Richmond, VA, USA, 1994.
39. Kayser, K., Bovin, N.V., Zemlyanukhina, T.V., Donaldo-Jacinto, S., Koopmann, J., Gabius, H.-J. Cell type-dependent alterations of binding of synthetic blood group antigen-related oligosaccharides in lung cancer. Glycoconjugate J. 11:339-344, 1994.
40. Wright, C.S. Histidine determination in wheat germ agglutinin isolectin by X-ray diffraction analysis. J. Mol. Biol. 145:453-461, 1981.
41. Zheng, J., Schodel, F., Peterson, D.L. The structure of hepadnaviral core antigens. J. Biol. Chem. 267:9422-9429, 1992.
42. Hagler, A.T., Huler, E., Lifson, S. Energy functions for peptides and proteins: Deviation of a consistent force field including the hydrogen bond for amide crystals. J. Am. Chem. Soc. 96:5316-5327, 1974.
43. Hagler, A.T., Lifson, S., Dauber, P. Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 2. A benchmark for the objective comparison of alternative force fields. J. Am. Chem. Soc. 101:5122-5130, 1979.
44. van Gunsteren, W.F. "GROMOS, Groningen Molecular Simulation Package." University of Groningen, The Netherlands, 1987.
45. van Gunsteren, W.F. The role of computer simulation techniques in protein engineering. Protein Eng 2:5-13, 1988.
46. Peitsch, M.C. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Transact. 24:274-279, 1996.
47. Lee, B., Richards, F.M. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55:379-400, 1971.
48. Kellenbach, E., Härd, T., Boelens, R., Dahlman, K., Carlstedt-Duke, J., Gustafsson, J-Å., van der Marel, G. A., van Boom, J.H., Maler, B., Yamamoto, K.R., Kaptein, R. Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements. J. Biomol. NMR 1:105-110, 1991.
49. Connolly, M.L. Analytical molecular surface calculation. J. Appl. Crystallogr. 16:548-558, 1983.
50. Connolly, M.L. Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713, 1983.
51. Edward, J.T. Molecular volumes and the Stokes-Einstein equation. J. Chem. Educ. 47:261-270, 1970.
52. Andersen, N.H., Cao, B., Rodriguez-Romero, A., Arreguin, B. Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif. Biochemistry 32:1407-1422, 1993.
53. Asensio, J.L., Canada, F.J., Bruix, M., Rodriguez-Romero, A., Jimenez-Barbero, J. The interaction of hevein with N-acetylglucosamine-containing oligosaccharides: Solution structure of hevein complexed with chitobiose. Eur. J. Biochem. 230:621-633, 1994.
54. Rodriguez-Romero, A., Ravichandran, K.G., Soriana-Garcia, M. Crystal structure of hevein at 2.8 Å resolution. FEES Lett. 291:307-309, 1995.
55. Horn, K., Gochin, M., Peumans, W.J., Shine, N. Ligand-induced perturbations in Urtica dioica agglutinin. FEBS Lett. 361:157-161, 1995.
56. Komano, H., Kurama, T., Nagasawa, Y., Natori, S. Evidence for an increase in positive surface charge and an increase in susceptibility to trypsin of Sarcophaga lectin (from flesh fly, Sarcophaga peregrina) on its interaction with galactose, a hapten sugar of the lectin. Biochem. J. 284:227-230, 1992.
57. Efting, M.R., Anusiem, A.C., Biltonen, R.L. Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry 22:3884-3896, 1983.
58. Perez, S., Imberty, A., Carver, J. Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides. Adv. Comput. Biol. 1:147-202, 1994.
59. Shrive, A.K., Cheetham, G.M.T., Holden, D., Myles, D.A.A., Turnell, W.G., Volanakis, J.E., Pepys, M.B., Bloomer, A.C., Greenhough, T.J. Three dimensional structure of human C-reactive protein. Nature Struct. Biol. 3:346-354, 1996.
60. Siebert, H.-C., Kaptein, R., Vliegenthart J.F.G. Study of oligosaccharide-lectin interaction by various nuclear magnetic resonance (NMR) techniques and computational methods. In: "Lectins and Glycobiology." Gabius, H.-J., Gabius, S. (eds.). New York: Springer-Verlag, 1993:105-116.
61. Siebert, H.-C., Gilleron, M., Kaltner, H., von der Lieth, C.-W., Kozàr, T., Bovin, N.V., Korchagina, E.Y., Vliegenthart, J.F. G., Gabius H.-J. NMR-based, molecular dynamics and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galβ1,2Galβ1-R) for an animal galectin in the free and in the bound state. Biochem. Biophys. Res. Commun. 219:205-212, 1996.
62. Siebert, H.-C., von der Lieth, C.-W., Gilleron, M., Reuter, G., Wittmann, J., Vliegenthart, J.F.G., Gabius, H.-J. Carbohydrate-protein interaction. In: "Glycosciences: Status and Perspectives." Gabius, H.-J., Gabius, S. (eds.). Weinheim: Chapman & Hall. 1997:291-310.
63. D1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids. Glycobiology 6:561-572, 1996.
64. van Halbeek, H. NMR development in structural studies of carbohydrates and their complexes. Curr. Opin. Struct. Biol. 4:697-709, 1994.
65. von der Lieth, C.-W., Kozár, T., Hull, W.E. A (critical) survey of modeling protocols used to explore the conformational space of oligosaccharides. J. Mol. Struct. (Theochem), in press, 1997.
66. Brooks, R.B., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathan, S., Karplus, M. CHARMM: A program for macromolecular energy minimization and dynamic calculations. J. Comput. Chem.4:187-217, 1983.