메뉴 건너뛰기




Volumn 8, Issue 5, 1999, Pages 1075-1086

Structural bases of lectin-carbohydrate affinities: Comparison with protein-folding energetics

Author keywords

Enthalpy; Entropy; Hydrogen bonding; Lectin carbohydrate association; Protein folding

Indexed keywords

CARBOHYDRATE; LECTIN;

EID: 0040040750     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.5.1075     Document Type: Article
Times cited : (50)

References (67)
  • 1
    • 0030917908 scopus 로고    scopus 로고
    • Loss of translational entropy in binding, folding, and catalysis
    • Amzel LM. 1997. Loss of translational entropy in binding, folding, and catalysis. Proteins Struct Funct Genet 28:144-149.
    • (1997) Proteins Struct Funct Genet , vol.28 , pp. 144-149
    • Amzel, L.M.1
  • 2
    • 0029013978 scopus 로고
    • The interaction of hevein with N-acetylglucosamine-containing oligosaccharides: Solution structure of hevein complexed to chitobiose
    • Asensio JL, Cañada FJ, Bruix M, Rodríguez-Romero A, Jiménez-Barbero J. 1995. The interaction of hevein with N-acetylglucosamine-containing oligosaccharides: Solution structure of hevein complexed to chitobiose. Eur J Biochem 230:621-633.
    • (1995) Eur J Biochem , vol.230 , pp. 621-633
    • Asensio, J.L.1    Cañada, F.J.2    Bruix, M.3    Rodríguez-Romero, A.4    Jiménez-Barbero, J.5
  • 3
    • 0027098042 scopus 로고
    • Microcalorimetric study of wheat germ agglutinin binding to N-acetylglucosamine and its oligomers
    • Bains G, Lee RT, Lee YC, Freire E. 1992. Microcalorimetric study of wheat germ agglutinin binding to N-acetylglucosamine and its oligomers. Biochemistry 31:12624-12628.
    • (1992) Biochemistry , vol.31 , pp. 12624-12628
    • Bains, G.1    Lee, R.T.2    Lee, Y.C.3    Freire, E.4
  • 4
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase
    • Baker BM, Murphy KP. 1997. Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase. J Mol Biol 268:557-569.
    • (1997) J Mol Biol , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 5
    • 0029997826 scopus 로고    scopus 로고
    • Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex
    • Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M. 1996. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex. J Mol Biol 259:281-296.
    • (1996) J Mol Biol , vol.259 , pp. 281-296
    • Banerjee, R.1    Das, K.2    Ravishankar, R.3    Suguna, K.4    Surolia, A.5    Vijayan, M.6
  • 6
    • 0030905238 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of HIV-1 protease inhibitors
    • Bardi JS, Luque I, Freire E. 1997. Structure-based thermodynamic analysis of HIV-1 protease inhibitors. Biochemistry 36:6588-6596.
    • (1997) Biochemistry , vol.36 , pp. 6588-6596
    • Bardi, J.S.1    Luque, I.2    Freire, E.3
  • 7
    • 6244250502 scopus 로고
    • The role of hydrogen bonds in protein folding and protein association
    • Ben-Naim A. 1991. The role of hydrogen bonds in protein folding and protein association. J Phys Chem 95:1437-1444.
    • (1991) J Phys Chem , vol.95 , pp. 1437-1444
    • Ben-Naim, A.1
  • 9
    • 0025670519 scopus 로고
    • Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: Fine specificity of the monosaccharide-binding site
    • Bourne Y, Rougé P, Cambillau C. 1990. Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: Fine specificity of the monosaccharide-binding site. Proteins Struct Funct Genet 8:365-376.
    • (1990) Proteins Struct Funct Genet , vol.8 , pp. 365-376
    • Bourne, Y.1    Rougé, P.2    Cambillau, C.3
  • 10
    • 0031030835 scopus 로고    scopus 로고
    • Energetics of cyclic crystal packing and solvation
    • Brady GP, Sharp KA. 1997. Energetics of cyclic crystal packing and solvation. Biophys J 72:913-927.
    • (1997) Biophys J , vol.72 , pp. 913-927
    • Brady, G.P.1    Sharp, K.A.2
  • 12
    • 9944232242 scopus 로고
    • Group contributions to the thermodynamics properties of non-ionic organic solutes in dilute aqueous solution
    • Cabani S, Gianni P, Mollica V, Lepori L. 1981. Group contributions to the thermodynamics properties of non-ionic organic solutes in dilute aqueous solution. J Sol Chem 10:563-595.
    • (1981) J Sol Chem , vol.10 , pp. 563-595
    • Cabani, S.1    Gianni, P.2    Mollica, V.3    Lepori, L.4
  • 13
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia C. 1976. The nature of the accessible and buried surfaces in proteins. J Mol Biol 105:1-14.
    • (1976) J Mol Biol , vol.105 , pp. 1-14
    • Chothia, C.1
  • 16
    • 0027196879 scopus 로고
    • Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 Å resolution
    • Delbaere LTJ, Vandonselaar M, Prasad L, Quail JW, Wilson KS, Dauter Z. 1993. Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 Å resolution. J Mol Biol 230:950-965.
    • (1993) J Mol Biol , vol.230 , pp. 950-965
    • Delbaere, L.T.J.1    Vandonselaar, M.2    Prasad, L.3    Quail, J.W.4    Wilson, K.S.5    Dauter, Z.6
  • 17
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig AJ, Sternberg MJE. 1995. Side-chain conformational entropy in protein folding. Protein Sci 4:2247-2251.
    • (1995) Protein Sci , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.E.2
  • 18
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • Finkelstein AV, Janin J. 1989. The price of lost freedom: Entropy of bimolecular complex formation. Protein Eng 3:1-3.
    • (1989) Protein Eng , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 19
    • 0029132790 scopus 로고
    • Thermodynamics of partly folded intermediates in proteins
    • Freire E. 1995. Thermodynamics of partly folded intermediates in proteins. Annu Rev Biophys Biomol Struct 24:141-165.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 141-165
    • Freire, E.1
  • 20
    • 0042617649 scopus 로고    scopus 로고
    • New insights into the molecular basis of lectin-carbohydrate interactions: A calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine
    • Garcia-Hernândez E, Zubillaga RA, Rojo-Domínguez A, Rodríguez-Romero A, Hernández-Arana A. 1997. New insights into the molecular basis of lectin-carbohydrate interactions: A calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine. Proteins Struct Funct Genet 29:467-477.
    • (1997) Proteins Struct Funct Genet , vol.29 , pp. 467-477
    • Garcia-Hernândez, E.1    Zubillaga, R.A.2    Rojo-Domínguez, A.3    Rodríguez-Romero, A.4    Hernández-Arana, A.5
  • 21
    • 0030024844 scopus 로고
    • Structure solution of a cubic crystal of concanavalin A complexed with methyl-α-D-glucopyranoside
    • Harrop SJ, Helliwell JR, Wan TCM, Kalb(Gilboa) AJ, Tong L, Yariv J. 1995. Structure solution of a cubic crystal of concanavalin A complexed with methyl-α-D-glucopyranoside. Acta Crystallogr D 52:143-145.
    • (1995) Acta Crystallogr D , vol.52 , pp. 143-145
    • Harrop, S.J.1    Helliwell, J.R.2    Wan, T.C.M.3    Kalb, A.J.4    Tong, L.5    Yariv, J.6
  • 22
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 23
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G, Kaku H, Goldstein IJ, Wright CS. 1995. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nature Struct Biol 2:472-479.
    • (1995) Nature Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 24
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin
    • Hirabayashi J, Kasai K. 1991. Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin. J Biol Chem 266:23648-23653.
    • (1991) J Biol Chem , vol.266 , pp. 23648-23653
    • Hirabayashi, J.1    Kasai, K.2
  • 25
    • 0029050481 scopus 로고
    • The "cratic correction" and related fallacies
    • Holtzer A. 1995. The "cratic correction" and related fallacies. Biopolymers 35:595-602.
    • (1995) Biopolymers , vol.35 , pp. 595-602
    • Holtzer, A.1
  • 26
    • 0027159280 scopus 로고
    • Oligosaccharides and recognition: A "shape" problem probed by n.m.r. and molecular modelling
    • Homans SW, Rutherford T. 1993. Oligosaccharides and recognition: A "shape" problem probed by n.m.r. and molecular modelling. Biochem Soc Trans 21:449-452.
    • (1993) Biochem Soc Trans , vol.21 , pp. 449-452
    • Homans, S.W.1    Rutherford, T.2
  • 27
    • 0003742069 scopus 로고
    • London UK: Department of Biochemistry and Molecular Biology, University College
    • Hubbard SJ, Thornton JM. 1993. NACCESS computer program. London UK: Department of Biochemistry and Molecular Biology, University College.
    • (1993) NACCESS Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 28
    • 0030834858 scopus 로고    scopus 로고
    • Oligosaccharide structures: Theory versus experiment
    • Imberty A. 1997. Oligosaccharide structures: Theory versus experiment. Curr Opin Struct Biol 7:617-623.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 617-623
    • Imberty, A.1
  • 29
    • 0028223728 scopus 로고
    • 2+-dependent animal lectins: II. Generation of high-affinity galactose binding by site-directed mutagenesis and NMR
    • 2+-dependent animal lectins: II. Generation of high-affinity galactose binding by site-directed mutagenesis and NMR. J Biol Chem 269:15512-15519.
    • (1994) J Biol Chem , vol.269 , pp. 15512-15519
    • Iobst, S.T.1    Drickamer, K.2
  • 30
    • 0028232179 scopus 로고
    • 2+-dependent animal lectins: I. Analysis of mannose binding by site-directed mutagenesis and NMR
    • 2+-dependent animal lectins: I. Analysis of mannose binding by site-directed mutagenesis and NMR. J Biol Chem 269:15505-15511.
    • (1994) J Biol Chem , vol.269 , pp. 15505-15511
    • Iobst, S.T.1    Wormald, M.R.2    Weis, W.I.3    Dwek, R.A.4    Drickamer, K.5
  • 32
    • 0029094346 scopus 로고
    • Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics
    • Lazaridis T, Archontis G, Karplus M. 1995. Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics. Adv Protein Chem 47:231-306.
    • (1995) Adv Protein Chem , vol.47 , pp. 231-306
    • Lazaridis, T.1    Archontis, G.2    Karplus, M.3
  • 33
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static stability
    • Lee B. Richards FM. 1971. The interpretation of protein structures: Estimation of static stability. J Mol Biol 55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 34
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian β-galactosides
    • Leffler H, Barondes SH. 1986. Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian β-galactosides. J Biol Chem 261:10119-10126.
    • (1986) J Biol Chem , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 35
    • 0003012148 scopus 로고    scopus 로고
    • How water provides the impetus for molecular recognition in aqueous solution
    • Lemieux RU. 1996. How water provides the impetus for molecular recognition in aqueous solution. Acc Chem Res 29:373-380.
    • (1996) Acc Chem Res , vol.29 , pp. 373-380
    • Lemieux, R.U.1
  • 36
    • 0027958144 scopus 로고
    • Structure of s-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O. 1994. Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein. Proc Natl Acad Sci USA 91:1428-1432.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 38
    • 0028206798 scopus 로고
    • Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin A
    • Mandal DK, Kishore N, Brewer CF. 1994. Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin A. Biochemistry 33:1149-1156.
    • (1994) Biochemistry , vol.33 , pp. 1149-1156
    • Mandal, D.K.1    Kishore, N.2    Brewer, C.F.3
  • 39
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald YK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, Y.K.1    Thornton, J.M.2
  • 41
    • 0028123001 scopus 로고
    • Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT)
    • Merritt EA, Sixma TK, Kalk KH, van Zanten BAM, Hol WGJ. 1994b. Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol Microbiol 13:745-753.
    • (1994) Mol Microbiol , vol.13 , pp. 745-753
    • Merritt, E.A.1    Sixma, T.K.2    Kalk, K.H.3    Van Zanten, B.A.M.4    Hol, W.G.J.5
  • 42
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP, Freire E. 1992. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 43:313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 45
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • Naghibi H, Tamura A, Sturtevant JM. 1995. Significant discrepancies between van't Hoff and calorimetric enthalpies. Proc Natl Acad Sci USA 92:5597-5599.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5597-5599
    • Naghibi, H.1    Tamura, A.2    Sturtevant, J.M.3
  • 47
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • Naismith JH, Field RA. 1996. Structural basis of trimannoside recognition by concanavalin A. J Biol Chem 271:972-976.
    • (1996) J Biol Chem , vol.271 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 48
    • 0030069340 scopus 로고    scopus 로고
    • Structural analysis of monosaccharide recognition by rat liver mannose-binding protein
    • Ng KKS, Drickamer K, Weis W. 1996. Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. J Biol Chem 271:663-674.
    • (1996) J Biol Chem , vol.271 , pp. 663-674
    • Ng, K.K.S.1    Drickamer, K.2    Weis, W.3
  • 49
    • 0000149999 scopus 로고
    • Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides
    • Pérez S, Imberty A, Carver JP. 1994. Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides. Adv Comp Biol 1:147-202.
    • (1994) Adv Comp Biol , vol.1 , pp. 147-202
    • Pérez, S.1    Imberty, A.2    Carver, J.P.3
  • 50
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II. The entropy and gibbs energy of hydration
    • Privalov PL, Makhatadze GI. 1993. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J Mol Biol 232:660-679.
    • (1993) J Mol Biol , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 51
    • 0029035874 scopus 로고
    • Energetics of carbohydrate binding by a 14 kDa s-type mammalian lectin
    • Ramkumar R, Surolia A, Podder SK. 1995. Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin. Biochem J 308:237-241.
    • (1995) Biochem J , vol.308 , pp. 237-241
    • Ramkumar, R.1    Surolia, A.2    Podder, S.K.3
  • 53
    • 0027314952 scopus 로고
    • X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 Å resolution
    • Rini JM, Hardman KD, Einspahr H, Suddath FL, Carver JP. 1993. X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 Å resolution. J Biol Chem 268:10126-10132.
    • (1993) J Biol Chem , vol.268 , pp. 10126-10132
    • Rini, J.M.1    Hardman, K.D.2    Einspahr, H.3    Suddath, F.L.4    Carver, J.P.5
  • 54
    • 0029889130 scopus 로고    scopus 로고
    • Effect of substituent on the thermodynamics of D-glucopyranoside binding to concanavalin A, pea (Pisum sativum) lectin and lentil (Lens culinaris) lectin
    • Schwarz FP, Misquith S, Surolia A. 1996. Effect of substituent on the thermodynamics of D-glucopyranoside binding to concanavalin A, pea (Pisum sativum) lectin and lentil (Lens culinaris) lectin. Biochem J 316:123-129.
    • (1996) Biochem J , vol.316 , pp. 123-129
    • Schwarz, F.P.1    Misquith, S.2    Surolia, A.3
  • 55
    • 0027538064 scopus 로고
    • Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin
    • Schwarz FP, Puri KD, Bhat RG, Surolia A. 1993. Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin. J Biol Chem 268:7668-7677.
    • (1993) J Biol Chem , vol.268 , pp. 7668-7677
    • Schwarz, F.P.1    Puri, K.D.2    Bhat, R.G.3    Surolia, A.4
  • 56
    • 9644258919 scopus 로고
    • The cost of conformational order: Entropy changes in molecular associations
    • Searle MS, Williams DH. 1992. The cost of conformational order: Entropy changes in molecular associations. J Am Chem Soc 114:10690-10697.
    • (1992) J Am Chem Soc , vol.114 , pp. 10690-10697
    • Searle, M.S.1    Williams, D.H.2
  • 57
    • 0027054352 scopus 로고
    • Partitioning of free energy contributions in the estimation of binding constants: Residual motions and consequences for amide-amide hydrogen bond strengths
    • Searle MS, Williams DH, Gerhard U. 1992. Partitioning of free energy contributions in the estimation of binding constants: Residual motions and consequences for amide-amide hydrogen bond strengths. J Am Chem Soc 114:10697-10704.
    • (1992) J Am Chem Soc , vol.114 , pp. 10697-10704
    • Searle, M.S.1    Williams, D.H.2    Gerhard, U.3
  • 58
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan B, Lis H, Sharon N. 1991. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254:862-866.
    • (1991) Science , vol.254 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 59
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • Sharon N, Lis H. 1989. Lectins as cell recognition molecules. Science 246:227-234.
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 60
    • 0030045734 scopus 로고    scopus 로고
    • 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
    • Siebert H-C, Gilleron M, Kaltner H, von der Lieth C-W, Kozár T, Bovin N, Korchagina EY, Vliegenthart JFG, Gabius H-J. 1996. 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 Comm 219:205-212.
    • (1996) Biochem Biophys Res Comm , vol.219 , pp. 205-212
    • Siebert, H.-C.1    Gilleron, M.2    Kaltner, H.3    Von Der Lieth, C.-W.4    Kozár, T.5    Bovin, N.6    Korchagina, E.Y.7    Vliegenthart, J.F.G.8    Gabius, H.-J.9
  • 62
    • 0029929718 scopus 로고    scopus 로고
    • Thermodynamics of monosaccharide and disaccharide binding to erythrina corallodendron lectin
    • Surolia A, Sharon N, Schwarz FP. 1996. Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin. J Biol Chem 271:17697-17703.
    • (1996) J Biol Chem , vol.271 , pp. 17697-17703
    • Surolia, A.1    Sharon, N.2    Schwarz, F.P.3
  • 63
    • 33845551411 scopus 로고
    • Geometry of the N-H···O=C hydrogen bond. 1. Lone-pair directionality
    • Taylor R, Kennard O, Versichel W. 1983. Geometry of the N-H···O=C hydrogen bond. 1. Lone-pair directionality. J Am Chem Soc 105:5761-5766.
    • (1983) J Am Chem Soc , vol.105 , pp. 5761-5766
    • Taylor, R.1    Kennard, O.2    Versichel, W.3
  • 65
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis WI, Drickamer K. 1996. Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem 65:441-473.
    • (1996) Annu Rev Biochem , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 66
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K, Hendrickson WA. 1992. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360:127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 67
    • 0029658497 scopus 로고    scopus 로고
    • The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes
    • Wright CS, Hester G. 1996. The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes. Structure 15:1339-1352.
    • (1996) Structure , vol.15 , pp. 1339-1352
    • Wright, C.S.1    Hester, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.