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Volumn 262, Issue 4, 1996, Pages 516-531

The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 Å and 3.0 Å resolution

Author keywords

Lectins; Mannose specificity; Saccharide binding; Snowdrop

Indexed keywords

AGGLUTININ; CARBOHYDRATE; DISACCHARIDE; LECTIN; MANNOSE; MANNOSIDE; OLIGOSACCHARIDE; PROTEIN SUBUNIT;

EID: 0030568976     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0532     Document Type: Article
Times cited : (82)

References (34)
  • 1
    • 0026020005 scopus 로고
    • α(1,3) and α-(1,6) mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro
    • Balzarini, J., Schols, D., Neyts, J., Van Damme, E. J. M., Peumans, W. & De Clercq, E. (1991). α(1,3) and α-(1,6) mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob. Agents. Chemother. 35, 410-416.
    • (1991) Antimicrob. Agents. Chemother. , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.J.M.4    Peumans, W.5    De Clercq, E.6
  • 2
    • 0029151455 scopus 로고
    • The structure of satellite pamicum mosaic virus at 1.9 Å resolution
    • Ban, N. & McPherson, A. (1995). The structure of satellite pamicum mosaic virus at 1.9 Å resolution. Nature Struct. Biol. 2, 882-890.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 882-890
    • Ban, N.1    McPherson, A.2
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992a). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 6
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 9
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 10
    • 0028972337 scopus 로고
    • Strange bedfellows: Interactions between acidic side-chains in proteins
    • Flocco, M. M. & Mowbray, S. L. (1995). Strange bedfellows: interactions between acidic side-chains in proteins. J. Mol. Biol. 254, 96-105.
    • (1995) J. Mol. Biol. , vol.254 , pp. 96-105
    • Flocco, M.M.1    Mowbray, S.L.2
  • 11
    • 0002199711 scopus 로고
    • Isolation, physiochemical characterization, and carbohydrate-binding specificity of lectins
    • (Liener, I. E., Sharon, N. & Goldstein, I. J., eds), Academic Press, Orlando, FL
    • Goldstein, I. J. & Poretz, R. D. (1986). Isolation, physiochemical characterization, and carbohydrate-binding specificity of lectins. In The Lectins: Properties, Function and Application in Biology and Medicine (Liener, I. E., Sharon, N. & Goldstein, I. J., eds), pp. 43-247, Academic Press, Orlando, FL.
    • (1986) The Lectins: Properties, Function and Application in Biology and Medicine , pp. 43-247
    • Goldstein, I.J.1    Poretz, R.D.2
  • 12
    • 0002860357 scopus 로고
    • Incorporation of stereochemical information into crystallographic refinement
    • (Diamond, R., Ramaseshan, S. & Venkatesan, K., eds), Indian Academy of Science, Bangalore
    • Hendrickson, W. A. & Konnert, J. H, (1980). Incorporation of stereochemical information into crystallographic refinement. In Computing in Crystallography (Diamond, R., Ramaseshan, S. & Venkatesan, K., eds), pp. 13.01-13.23, Indian Academy of Science, Bangalore.
    • (1980) Computing in Crystallography , pp. 1301-1323
    • Hendrickson, W.A.1    Konnert, J.H.2
  • 13
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester, G., Kaku, H., Goldstein, I. J. & Wright, C. S. (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
  • 14
    • 0025366497 scopus 로고
    • Data bank of three-dimensional structures of disaccharides, A tool to build 3-D structures of oligosaccharides
    • Imberty, A, Gerber, S., Tran, V. & Pérez, S. (1990). Data bank of three-dimensional structures of disaccharides, A tool to build 3-D structures of oligosaccharides. Glycoconjug. J. 7, 27-54.
    • (1990) Glycoconjug. J. , vol.7 , pp. 27-54
    • Imberty, A.1    Gerber, S.2    Tran, V.3    Pérez, S.4
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976). A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A, 32, 922-923.
    • (1976) Acta Crystallog. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 18
    • 0026170577 scopus 로고
    • Interactions of five D-mannose-specific lectins with a series of synthetic branched trisaccharides
    • Kaku, H. & Goldstein, I. J. (1991). Interactions of five D-mannose-specific lectins with a series of synthetic branched trisaccharides. Carbohyd. Res. 213, 109-116.
    • (1991) Carbohyd. Res. , vol.213 , pp. 109-116
    • Kaku, H.1    Goldstein, I.J.2
  • 19
    • 0026866642 scopus 로고
    • Interaction of linear manno-oligosaccharides with three mannose-specific bulb lectins. Comparison with mannose-glucose binding lectins
    • Kaku, H. & Goldstein, I. J. (1992). Interaction of linear manno-oligosaccharides with three mannose-specific bulb lectins. Comparison with mannose-glucose binding lectins. Carbohyd. Res. 229, 337-346.
    • (1992) Carbohyd. Res. , vol.229 , pp. 337-346
    • Kaku, H.1    Goldstein, I.J.2
  • 20
    • 0026170577 scopus 로고
    • Interaction of five D-mannose specific lectins with a series of synthetic branched trisaccharides
    • Kaku, H., Goldstein, I. J. & Oscarson, S. (1991). Interaction of five D-mannose specific lectins with a series of synthetic branched trisaccharides. Carbohyd. Res. 213, 109-116.
    • (1991) Carbohyd. Res. , vol.213 , pp. 109-116
    • Kaku, H.1    Goldstein, I.J.2    Oscarson, S.3
  • 21
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 24
    • 0001099937 scopus 로고
    • Traitements statistique des erreurs dans la détermination des structures cristallines
    • Luzzati, P. V. (1952). Traitements statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5, 802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 25
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merrit, E. A. & Murphy, M. E. P. (1994). Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D, 50, 869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 26
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A, 50, 157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S. S., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data collection and Processing (Sawyer, L., Isaacs, N. & Bailey, S. S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 28
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A, 42, 140-149.
    • (1986) Acta Crystallog. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 29
    • 0027158038 scopus 로고
    • Lectin-carbohydrate complexes of plants and animals: An atomic view
    • Sharon, N. (1993). Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biochem. Sci. 18, 221-226.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 221-226
    • Sharon, N.1
  • 30
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from snowdrop (Galanthus nivalis) bulb
    • Shibuya, N., Goldstein, I. J., Van Damme, E. J. M. & Peumans, W. Y. (1988). Binding properties of a mannose-specific lectin from snowdrop (Galanthus nivalis) bulb. J. Biol. Chem. 263, 728-734.
    • (1988) J. Biol. Chem. , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.M.3    Peumans, W.Y.4
  • 33
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W. I., Drickamer, K. & Hendrickson, W. A. (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
  • 34
    • 0025174183 scopus 로고
    • Crystallization and preliminary X-ray diffraction results of snowdrop (Galanthus nivalis) lectin
    • Wright, C. S., Kaku, H. & Goldstein, I. J. (1990). Crystallization and preliminary X-ray diffraction results of snowdrop (Galanthus nivalis) lectin. J. Biol. Chem. 265, 1676-1677.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1676-1677
    • Wright, C.S.1    Kaku, H.2    Goldstein, I.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.