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Volumn 5, Issue 8, 1998, Pages 427-437

A molecular basis for glycosylation-induced conformational switching

Author keywords

Glycopeptide; Hemagglutinin; Peptide conformation; Turn

Indexed keywords

INFLUENZA VIRUS;

EID: 0032146060     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90159-4     Document Type: Article
Times cited : (100)

References (48)
  • 1
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek, R.A. (1996). Glycobiology: toward understanding the function of sugars. Chem. Rev, 96, 683-720.
    • (1996) Chem. Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 2
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993). Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 3
    • 0030267033 scopus 로고    scopus 로고
    • Modulation of protein structure and function by asparagine-linked glycosylation
    • O'Connor, S. E. & Imperiali, B. (1996). Modulation of protein structure and function by asparagine-linked glycosylation. Chem. Biol. 3, 803-812.
    • (1996) Chem. Biol. , vol.3 , pp. 803-812
    • O'Connor, S.E.1    Imperiali, B.2
  • 4
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • Wyss, D.F. & Wagner, G. (1996). The structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 7, 409-416.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, G.2
  • 5
    • 0030799062 scopus 로고    scopus 로고
    • Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells
    • Lehman, S. & Harris, D.A. (1997). Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479-21487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21479-21487
    • Lehman, S.1    Harris, D.A.2
  • 6
    • 0029095485 scopus 로고
    • Structure and function of corticosteroid-binding globulin: Role of carbohydrates
    • Awakumov, G.V. (1995). Structure and function of corticosteroid-binding globulin: role of carbohydrates. J. Steroid Biochem. 53, 515-522.
    • (1995) J. Steroid Biochem. , vol.53 , pp. 515-522
    • Awakumov, G.V.1
  • 7
    • 0028899494 scopus 로고
    • Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein
    • Hu, A., Cathomen, T., Cattaneo, R. & Norrby, E. (1995). Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein. J. Gen. Virol. 76, 705-710.
    • (1995) J. Gen. Virol. , vol.76 , pp. 705-710
    • Hu, A.1    Cathomen, T.2    Cattaneo, R.3    Norrby, E.4
  • 8
    • 0029005022 scopus 로고
    • The saccharide chain of lupin seed conglutin γ is not responsible for the protection of the native protein from degradation by trypsin, but facilitates the refolding of the acid treated protein to the resistant conformation
    • Duranti, M., Gius, C., Sessa, F. & Vecchio, G. (1995). The saccharide chain of lupin seed conglutin γ is not responsible for the protection of the native protein from degradation by trypsin, but facilitates the refolding of the acid treated protein to the resistant conformation. Eur. J. Biochem. 230, 886-891.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 886-891
    • Duranti, M.1    Gius, C.2    Sessa, F.3    Vecchio, G.4
  • 9
    • 0029040839 scopus 로고
    • The asparagine-linked oligosaccharides of the human chorionic gonadotropin β subunit facilitate correct disulfide bond pairing
    • Feng, W., Matzuk, M.M., Mountjoy, K., Bedows, E., Ruddon, R.W. & Boime, I. (1995). The asparagine-linked oligosaccharides of the human chorionic gonadotropin β subunit facilitate correct disulfide bond pairing. J. Biol. Chem. 270, 11851-11859.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11851-11859
    • Feng, W.1    Matzuk, M.M.2    Mountjoy, K.3    Bedows, E.4    Ruddon, R.W.5    Boime, I.6
  • 10
    • 0027507503 scopus 로고
    • Kinetics of folding and association of differently glycosylated variants of invertase from S. cerevisiae
    • Kern, G., Kern, D., Jaenicke, R. & Seckler, R. (1993). Kinetics of folding and association of differently glycosylated variants of invertase from S. cerevisiae. Protein Sci. 2, 1862-1868.
    • (1993) Protein Sci. , vol.2 , pp. 1862-1868
    • Kern, G.1    Kern, D.2    Jaenicke, R.3    Seckler, R.4
  • 11
    • 0025770126 scopus 로고
    • Absence of asparagine-linked oligosaccharides from a glycoprotein D of herpes simplex virus type 1 results in a structurally altered but biologically active protein
    • Sodora, D.L., Cohen, G.H., Muggeridge, M.I. & Eisenberg, R.J. (1991). Absence of asparagine-linked oligosaccharides from a glycoprotein D of herpes simplex virus type 1 results in a structurally altered but biologically active protein. J. Virol. 65, 4424-4431.
    • (1991) J. Virol. , vol.65 , pp. 4424-4431
    • Sodora, D.L.1    Cohen, G.H.2    Muggeridge, M.I.3    Eisenberg, R.J.4
  • 12
    • 0031056089 scopus 로고    scopus 로고
    • Thermodynamics of unfolding for kazal-type serine protease inhibitors: Entropic stabilization of ovomucoid first domain by glycosylation
    • Dekoster, G.T. & Robertson, A.D. (1997). Thermodynamics of unfolding for kazal-type serine protease inhibitors: entropic stabilization of ovomucoid first domain by glycosylation. Biochemistry 36, 2323-2331.
    • (1997) Biochemistry , vol.36 , pp. 2323-2331
    • Dekoster, G.T.1    Robertson, A.D.2
  • 13
    • 0030940704 scopus 로고    scopus 로고
    • Conformational switching by asparagine-linked glycosylation
    • O'Connor, S.E. & Imperiali, B. (1997). Conformational switching by asparagine-linked glycosylation. J. Am. Chem. Soc. 119, 2295-2296.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2295-2296
    • O'Connor, S.E.1    Imperiali, B.2
  • 14
    • 0029803424 scopus 로고    scopus 로고
    • Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding
    • Live, D.H., Kumar, R A., Beebe, X. & Danishefsky, S.J. (1996). Conformational influences of glycosylation of a peptide: a possible model for the effect of glycosylation on the rate of protein folding. Proc. Natl Acad. Sci. USA. 93, 12759-12761.
    • (1996) Proc. Natl Acad. Sci. USA. , vol.93 , pp. 12759-12761
    • Live, D.H.1    Kumar, R.A.2    Beebe, X.3    Danishefsky, S.J.4
  • 15
    • 0028206748 scopus 로고
    • Attachment of oligosaccharides to peptide antigen profoundly affects binding to major histocompatibility complex class II molecules and peptide immunogenicity
    • Mouritsen, S., Meldal, M., Christiansenbrams, I., Eisner, H. & Werdelin, O. (1994). Attachment of oligosaccharides to peptide antigen profoundly affects binding to major histocompatibility complex class II molecules and peptide immunogenicity. Eur. J. Immun. 24, 1066-1072.
    • (1994) Eur. J. Immun. , vol.24 , pp. 1066-1072
    • Mouritsen, S.1    Meldal, M.2    Christiansenbrams, I.3    Eisner, H.4    Werdelin, O.5
  • 16
    • 13344291142 scopus 로고
    • Effects of glycosylation on peptide backbone conformation
    • Andreotti, A.H. & Kahne, D. (1993). Effects of glycosylation on peptide backbone conformation. J. Am. Chem. Soc. 115, 3352-3353.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3352-3353
    • Andreotti, A.H.1    Kahne, D.2
  • 17
    • 0028829350 scopus 로고
    • Glycobiology: The function of sugar in the IgG molecule
    • Dwek, R. A., Lellouch, A. C. & Wormald, M. R. (1995). Glycobiology: the function of sugar in the IgG molecule. J. Anat. 187, 279-292.
    • (1995) J. Anat. , vol.187 , pp. 279-292
    • Dwek, R.A.1    Lellouch, A.C.2    Wormald, M.R.3
  • 18
    • 0029133626 scopus 로고
    • Conformation and function of the N-linked glycan in the adhesion domain of human CD2
    • Wyss, D.F., et al., & Wagner, G. (1995). Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 269, 1273-1278.
    • (1995) Science , vol.269 , pp. 1273-1278
    • Wyss, D.F.1    Wagner, G.2
  • 19
    • 0001281325 scopus 로고
    • Conformation determining role for the N-acetyl group in the O-glycosidic linkage α-GalNAc-Thr
    • Maeji, N.J., Inoue, Y. & Chujo, R. (1987). Conformation determining role for the N-acetyl group in the O-glycosidic linkage α-GalNAc-Thr. Biopolymers 26, 1753-1767.
    • (1987) Biopolymers , vol.26 , pp. 1753-1767
    • Maeji, N.J.1    Inoue, Y.2    Chujo, R.3
  • 20
    • 0025062924 scopus 로고
    • One-dimensional and 2-dimensional NMR studies of the N-terminal portion of glycoporphorin-A at 11.7 Tesla
    • Dill, K., Hu, S., Berman, E., Pavia, A.A. & Lacombe, J. (1990). One-dimensional and 2-dimensional NMR studies of the N-terminal portion of glycoporphorin-A at 11.7 Tesla. J. Protein Chem. 9, 129-136.
    • (1990) J. Protein Chem. , vol.9 , pp. 129-136
    • Dill, K.1    Hu, S.2    Berman, E.3    Pavia, A.A.4    Lacombe, J.5
  • 21
  • 22
    • 0032577049 scopus 로고    scopus 로고
    • Convergent synthesis of N-linked glycopeptides on a solid support
    • Roberge, J.Y., Beebe, X. & Danishefsky, S.J. (1998). Convergent synthesis of N-linked glycopeptides on a solid support. J. Am. Chem. Soc. 120, 3915-3927.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3915-3927
    • Roberge, J.Y.1    Beebe, X.2    Danishefsky, S.J.3
  • 23
    • 0031323343 scopus 로고    scopus 로고
    • Synthetic methods of glycopeptide assembly and biological analysis of glycopeptide products
    • Meldal, M. & St Hilaire, P.M. (1997). Synthetic methods of glycopeptide assembly and biological analysis of glycopeptide products. Curr. Opin. Chem. Biol. 1, 552-563.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 552-563
    • Meldal, M.1    St Hilaire, P.M.2
  • 24
    • 0030670397 scopus 로고    scopus 로고
    • A strategy for the chemoselective synthesis of O-linked glycopeptides with native sugar-peptide linkages
    • Rodriguez, E.C., Winans, K.A., King, D.S. & Bertozzi, C.R. (1997). A strategy for the chemoselective synthesis of O-linked glycopeptides with native sugar-peptide linkages. J. Am. Chem. Soc. 119, 9905-9906.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9905-9906
    • Rodriguez, E.C.1    Winans, K.A.2    King, D.S.3    Bertozzi, C.R.4
  • 25
    • 0030936614 scopus 로고    scopus 로고
    • Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation
    • Witte, K., Sears, P., Martin, R. & Wong, C.H. (1997). Enzymatic glycoprotein synthesis: preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation. J. Am. Chem. Soc. 119, 2114-2118.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2114-2118
    • Witte, K.1    Sears, P.2    Martin, R.3    Wong, C.H.4
  • 26
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali, B. & Rickert, K.W. (1995). Conformational implications of asparagine-linked glycosylation. Proc. Natl Acad. Sci. USA 92, 97-101.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 27
    • 0022757887 scopus 로고
    • Do asparagine-linked carbohydrate chains have a preference for β-bends?
    • Beintema, J.J. (1986). Do asparagine-linked carbohydrate chains have a preference for β-bends? Biosci. Rep. 6, 709-714.
    • (1986) Biosci. Rep. , vol.6 , pp. 709-714
    • Beintema, J.J.1
  • 28
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright, P.E., Dyson, H.J. & Lerner, R.A. (1988). Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry 27, 7167-7175.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3
  • 29
    • 0001270462 scopus 로고
    • A practical, convergent method for glycopeptide synthesis
    • Cohen-Anisfeld, S.T. & Lansbury, P.T.J. (1993). A practical, convergent method for glycopeptide synthesis. J. Am. Chem. Soc. 115, 10531-10537.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10531-10537
    • Cohen-Anisfeld, S.T.1    Lansbury, P.T.J.2
  • 30
    • 0028266884 scopus 로고
    • Solid-phase N-glycopeptide synthesis using allyl sidechain protected fmoc-amino acids
    • Kates, S.A., de la Torre, B.C., Eritja, R. & Albericio, F. (1994). Solid-phase N-glycopeptide synthesis using allyl sidechain protected fmoc-amino acids. Tetrahedron Lett. 35, 1033-1034.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 1033-1034
    • Kates, S.A.1    De La Torre, B.C.2    Eritja, R.3    Albericio, F.4
  • 32
    • 0027957966 scopus 로고
    • Glycoforms modify the dynamic stability and functional activity of an enzyme
    • Rudd, P.M., et al., & Dwek, R.A. (1994). Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 33, 17-22.
    • (1994) Biochemistry , vol.33 , pp. 17-22
    • Rudd, P.M.1    Dwek, R.A.2
  • 33
    • 0025782587 scopus 로고
    • The conformation effects of N-glycosylation on the tailpiece from serum IgM
    • Wormald, M.R., et al., & Dwek, R.A. (1991). The conformation effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198, 131-139.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 131-139
    • Wormald, M.R.1    Dwek, R.A.2
  • 35
    • 0029670761 scopus 로고    scopus 로고
    • 13C NMR relaxation studies of backbone and sidechain motion of the catalytic tyrosine residue
    • 13C NMR relaxation studies of backbone and sidechain motion of the catalytic tyrosine residue. Biochemistry 35, 1525-1532.
    • (1996) Biochemistry , vol.35 , pp. 1525-1532
    • Zhao, Q.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 37
    • 33751384922 scopus 로고
    • Characterization of the extent of internal motions in oligosaccharides
    • Rutherford, T.J., Partridge, J., Weller, C.T. & Homans, S.W. (1993). Characterization of the extent of internal motions in oligosaccharides. Biochemistry 32, 12715-12724.
    • (1993) Biochemistry , vol.32 , pp. 12715-12724
    • Rutherford, T.J.1    Partridge, J.2    Weller, C.T.3    Homans, S.W.4
  • 38
    • 0019887973 scopus 로고
    • Structure and dynamics: Behavior of the oligosaccharide sidechain of bovine pancreatic ribonuclease B
    • Berman, E., Walters, D.E. & Allerhand, A. (1981). Structure and dynamics: behavior of the oligosaccharide sidechain of bovine pancreatic ribonuclease B. J. Biol. Chem. 256, 3853-3857.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3853-3857
    • Berman, E.1    Walters, D.E.2    Allerhand, A.3
  • 39
    • 0032539529 scopus 로고    scopus 로고
    • Mobilities at the inner 3 core residues and the man[α(1 -6)] branch of the glycan at Asn78 of the alpha subunit of human chorionic gonadotropin are restricted by the protein
    • Thisjssenvanzuylen, C.W.E.M., et al., & Vliegenthart, J.F.G. (1998). Mobilities at the inner 3 core residues and the man[α(1 -6)] branch of the glycan at Asn78 of the alpha subunit of human chorionic gonadotropin are restricted by the protein. Biochemistry 37, 1933-1940.
    • (1998) Biochemistry , vol.37 , pp. 1933-1940
    • Thisjssenvanzuylen, C.W.E.M.1    Vliegenthart, J.F.G.2
  • 40
    • 0031038310 scopus 로고    scopus 로고
    • Molecular motions of a glycopeptide from human serum transferrin studies by C-13 nuclear magnetic resonance
    • Lu, J.Y. & Vanhealbeek, H. (1997). Molecular motions of a glycopeptide from human serum transferrin studies by C-13 nuclear magnetic resonance. Biophys. J. 72, 470-481.
    • (1997) Biophys. J. , vol.72 , pp. 470-481
    • Lu, J.Y.1    Vanhealbeek, H.2
  • 41
    • 0029002994 scopus 로고
    • Structural fluctuation of methyl N,N-diacetyl-β-D-chitobioside in vacuo and in aqueous solution: Molecular dynamics and proton NMR spectroscopy
    • Aida, M., Sugawara, Y., Oikawa, S. & Umemoto, K. (1995). Structural fluctuation of methyl N,N-diacetyl-β-D-chitobioside in vacuo and in aqueous solution: molecular dynamics and proton NMR spectroscopy. Int. J. Macromol. 17, 227-235.
    • (1995) Int. J. Macromol. , vol.17 , pp. 227-235
    • Aida, M.1    Sugawara, Y.2    Oikawa, S.3    Umemoto, K.4
  • 42
    • 0000184586 scopus 로고
    • Molecular dynamics simulation of cellobiose in water
    • Hardy, B.J. & Sarko, A. (1993). Molecular dynamics simulation of cellobiose in water. J. Comp. Chem, 14, 848-857.
    • (1993) J. Comp. Chem , vol.14 , pp. 848-857
    • Hardy, B.J.1    Sarko, A.2
  • 43
    • 0000895332 scopus 로고
    • Involvement of side functions in peptide structures: The asx turn. Occurrence and conformational aspects
    • Abbadi, A., Mcharfi, M., Aubry, A., Premilat, S., Boussard, G. & Marraud, M. (1991). Involvement of side functions in peptide structures: the asx turn. Occurrence and conformational aspects. J. Am. Chem. Soc. 113, 2729-2735.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 2729-2735
    • Abbadi, A.1    Mcharfi, M.2    Aubry, A.3    Premilat, S.4    Boussard, G.5    Marraud, M.6
  • 44
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. & Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev, Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 45
    • 0030064740 scopus 로고    scopus 로고
    • Influence of core glycosylation on the flexibility of a biantennary N-linked oligosaccharide
    • Stubbs, H.J., Lih, J.J., Gustafson, T.L., Rice, K.G. (1996). Influence of core glycosylation on the flexibility of a biantennary N-linked oligosaccharide. Biochemistry 35, 937-947.
    • (1996) Biochemistry , vol.35 , pp. 937-947
    • Stubbs, H.J.1    Lih, J.J.2    Gustafson, T.L.3    Rice, K.G.4
  • 46
    • 1542576118 scopus 로고    scopus 로고
    • On resin solid phase synthesis of asparagine linked glycopeptides: Use of N-(2-acetoxy-4-methoxybenzyl) aspartyl amide bond protection to prevent unwanted aspartimide formation
    • Offer, J., Quibell, M. & Johnson, T. (1996). On resin solid phase synthesis of asparagine linked glycopeptides: use of N-(2-acetoxy-4-methoxybenzyl) aspartyl amide bond protection to prevent unwanted aspartimide formation. J. Chem. Soc. Perkin Trans. 1 175-182.
    • (1996) J. Chem. Soc. Perkin Trans. 1 , pp. 175-182
    • Offer, J.1    Quibell, M.2    Johnson, T.3
  • 48
    • 0000733545 scopus 로고
    • NMR Experiments for the measurement of carbon relaxation properties in highly enriched, uniformly C-13, N-15-labeled proteins: Application to C-13(alpha) carbons
    • Yamazaki, T., Munhandiram, R. & Kay, L.E. (1994). NMR Experiments for the measurement of carbon relaxation properties in highly enriched, uniformly C-13, N-15-labeled proteins: application to C-13(alpha) carbons. J. Am. Chem. Soc. 116, 8266-8278.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8266-8278
    • Yamazaki, T.1    Munhandiram, R.2    Kay, L.E.3


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