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Volumn 16, Issue 7, 2006, Pages 635-640

Structural basis of carbohydrate recognition by a Man(α1-2)Man-specific lectin from Bowringia milbraedii

Author keywords

Carbohaydrate recognition; Lectin; Legume lectin; X ray crystallography

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; CONCANAVALIN A; MANNOSE BINDING LECTIN; MONOSACCHARIDE; PLANT LECTIN; TETRAMER;

EID: 33745600570     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwj109     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 0024513424 scopus 로고
    • Bowringia milbraedii agglutinin. Specificity of binding to early processing intermediates of asparaginelinked oligosaceharide and use as a marker of endoplasmic reticulum glycoproteins
    • Animashaun, T. and Hughes, R.C. (1989) Bowringia milbraedii agglutinin. Specificity of binding to early processing intermediates of asparaginelinked oligosaceharide and use as a marker of endoplasmic reticulum glycoproteins. J. Biol. Chem., 264, 4657-4663.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4657-4663
    • Animashaun, T.1    Hughes, R.C.2
  • 2
    • 0018788748 scopus 로고
    • Mechanism of binding of mono and oligosaccharides to concanavalin A: A solvent proton magnetic relaxation dispersion study
    • Brewer, C.F. and Brown, R.D. (1979) Mechanism of binding of mono and oligosaccharides to concanavalin A: A solvent proton magnetic relaxation dispersion study. Biochemistry, 18, 2555-2562.
    • (1979) Biochemistry , vol.18 , pp. 2555-2562
    • Brewer, C.F.1    Brown, R.D.2
  • 4
    • 0035946982 scopus 로고    scopus 로고
    • Weak protein-protein interactions in lectins: The crystal structure of a vegetative lectin from the legume Dolichos biflorus
    • Buts, L., Dao-Thi, M.-H., Loris, R., Wyns, L., Etzler, M., and Hamelryck, T. (2001) Weak protein-protein interactions in lectins: The crystal structure of a vegetative lectin from the legume Dolichos biflorus. J. Mol. Biol., 309, 193-201.
    • (2001) J. Mol. Biol. , vol.309 , pp. 193-201
    • Buts, L.1    Dao-Thi, M.-H.2    Loris, R.3    Wyns, L.4    Etzler, M.5    Hamelryck, T.6
  • 5
    • 0032571487 scopus 로고    scopus 로고
    • Amino acid sequence, glycan structure, and proteolytic processing of the lectin of Vatairea macrocarpa seeds
    • Calvete, J.J., Santos, C.F., Mann, K., Grangeiro, T.B., Nimtzd, M., Urbanke, C., and Sousa-Cavada, B. (1998) Amino acid sequence, glycan structure, and proteolytic processing of the lectin of Vatairea macrocarpa seeds. FEBS Lett., 425, 286-292.
    • (1998) FEBS Lett. , vol.425 , pp. 286-292
    • Calvete, J.J.1    Santos, C.F.2    Mann, K.3    Grangeiro, T.B.4    Nimtzd, M.5    Urbanke, C.6    Sousa-Cavada, B.7
  • 7
    • 0026569915 scopus 로고
    • Interactions of Bowringia mildbraedii agglutinin with complex- and hybrid-type glycans
    • Chawla, D., Animashaun, T., and Hughes, R.C. (1992) Interactions of Bowringia mildbraedii agglutinin with complex- and hybrid-type glycans. FEBS Lett., 298, 291-296.
    • (1992) FEBS Lett. , vol.298 , pp. 291-296
    • Chawla, D.1    Animashaun, T.2    Hughes, R.C.3
  • 8
    • 0027183873 scopus 로고
    • Bowringia mildbraedii agglutinin: Polypeptide composition, primary structure and homologies with other legume lectins
    • Chawla, D., Animashaun, T., Hughes, R.C., Harris, A., and Aitken, A. (1993) Bowringia mildbraedii agglutinin: Polypeptide composition, primary structure and homologies with other legume lectins. Biochim. Biophys. Acta, 1202, 38-46.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 38-46
    • Chawla, D.1    Animashaun, T.2    Hughes, R.C.3    Harris, A.4    Aitken, A.5
  • 9
    • 84988115618 scopus 로고
    • Validation of the general-purpose TRIPOS 5.2 force-field
    • Clark, M., Cramer, R.D.I., and van den Opdenbosch, N. (1989) Validation of the general-purpose TRIPOS 5.2 force-field. J. Comput. Chem., 10, 982-1012.
    • (1989) J. Comput. Chem. , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer, R.D.I.2    van den Opdenbosch, N.3
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography Acta Crystallogr
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr., 50, 760-763.
    • (1994) D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 11
    • 0036462596 scopus 로고    scopus 로고
    • Thermodynamic studies of lectin-carbohydrate interactions by isothermal titration calorimetry
    • Dam, T.K. and Brewer, C.F. (2002) Thermodynamic studies of lectin-carbohydrate interactions by isothermal titration calorimetry. Chem. Rev., 102, 387-429.
    • (2002) Chem. Rev. , vol.102 , pp. 387-429
    • Dam, T.K.1    Brewer, C.F.2
  • 13
  • 15
    • 33744455474 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the Man(α1-2 )Man-specific lectin from Bowringia mildbraedii in complex with its carbohydrate ligand
    • Garcia-Pino, A., Loris, R., Wyns, L., and Buts, L. (2005) Crystallization and preliminary X-ray analysis of the Man(α1-2)Man-specific lectin from Bowringia mildbraedii in complex with its carbohydrate ligand. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 61, 931-934.
    • (2005) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.61 , pp. 931-934
    • Garcia-Pino, A.1    Loris, R.2    Wyns, L.3    Buts, L.4
  • 16
    • 0034674159 scopus 로고    scopus 로고
    • The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: Crystal structure of cross-linked FRIL
    • Hamelryck, T.W., Moore, J.G., Chrispeels, M.J., Loris, R., and Wyns, L. (2000) The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: Crystal structure of cross-linked FRIL. J. Mol. Biol., 299, 875-883.
    • (2000) J. Mol. Biol. , vol.299 , pp. 875-883
    • Hamelryck, T.W.1    Moore, J.G.2    Chrispeels, M.J.3    Loris, R.4    Wyns, L.5
  • 17
    • 0017232340 scopus 로고
    • Structure of the concanavalin A-methyl α-D-mannopyranoside complex at 6-A resolution
    • Hardman, K.D. and Ainsworth, C.F. (1976) Structure of the concanavalin A-methyl α-D-mannopyranoside complex at 6-A resolution. Biochemistry, 15, 1120-1128.
    • (1976) Biochemistry , vol.15 , pp. 1120-1128
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 18
    • 33745610391 scopus 로고
    • NACCESS [computer program]. Department of Biochemistry and Molecular Biology, University College London
    • Hubbard, S.J. and Thornton, J.M. (1993) NACCESS [computer program]. Department of Biochemistry and Molecular Biology, University College London.
    • (1993)
    • Hubbard, S.J.1    Thornton, J.M.2
  • 19
    • 0002555541 scopus 로고    scopus 로고
    • Building sugars: The sweet part of structural biology
    • Vijayan, M., Yathindra, N., Kolaskar, A.S. (eds), Indian Academy of Sciences and Universities Press, Hyderabad, India
    • Imberty, A., Bettler, E., Karababa, M., Mazeau, K., Petrova, P., and Perez, S. (1999) Building sugars: The sweet part of structural biology. In Vijayan, M., Yathindra, N., Kolaskar, A.S. (eds), Perspectives in Structural Biology. Indian Academy of Sciences and Universities Press, Hyderabad, India, pp. 392-409.
    • (1999) Perspectives in Structural Biology , pp. 392-409
    • Imberty, A.1    Bettler, E.2    Karababa, M.3    Mazeau, K.4    Petrova, P.5    Perez, S.6
  • 20
    • 0028200833 scopus 로고
    • Molecular modelling of protein-carbohydrate interactions. Understanding the specificities of two legume lectins towards oligosaccharides
    • Imberty, A. and Perez, S. (1994) Molecular modelling of protein-carbohydrate interactions. Understanding the specificities of two legume lectins towards oligosaccharides. Glycobiology, 4, 351-366.
    • (1994) Glycobiology , vol.4 , pp. 351-366
    • Imberty, A.1    Perez, S.2
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst., 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I.K., and Thornton, J.M. (1994) Satisfying hydrogen bonding potential in proteins. J. Mol. Biol., 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 26
    • 0028057108 scopus 로고
    • Raster3D, Version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A., and Murphy, M.E. (1994) Raster3D, Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr., 50, 869-873.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 27
    • 0032586737 scopus 로고    scopus 로고
    • Man(α1-2) Man(α-O)Me-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
    • Moothoo, D.N., Canan, B., Field, R.A., and Naismith, J.H. (1999) Man(α1-2) Man(α-O)Me-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology, 9, 539-545.
    • (1999) Glycobiology , vol.9 , pp. 539-545
    • Moothoo, D.N.1    Canan, B.2    Field, R.A.3    Naismith, J.H.4
  • 28
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • Naismith, J.H. and Field, R.A. (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
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0029379651 scopus 로고
    • Lectins as plant defense proteins
    • Peumans, W.J. and Van Damme, E.J.M. (1995) Lectins as plant defense proteins. Plant Physiol., 109, 347-352.
    • (1995) Plant Physiol. , vol.109 , pp. 347-352
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 31
    • 0016662479 scopus 로고
    • The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure
    • Reeke, G.N. Jr, Becker, J.W., and Edelman, G.M. (1975) The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure. J. Biol. Chem., 250, 1525-1547.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1525-1547
    • Reeke Jr., G.N.1    Becker, J.W.2    Edelman, G.M.3
  • 33
    • 0032484210 scopus 로고    scopus 로고
    • Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates
    • Rozwarski, D.A., Swami, B.M., Brewer, C.F., and Sacchettini, J.C. (1998) Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates. J. Biol Chem., 273; 32818-32825.
    • (1998) J. Biol Chem. , vol.273 , pp. 32818-32825
    • Rozwarski, D.A.1    Swami, B.M.2    Brewer, C.F.3    Sacchettini, J.C.4
  • 35
    • 0030995894 scopus 로고    scopus 로고
    • The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A
    • Sanz-Aparicio, J., Hermoso, J., Grangeiro, T.B., Calvete, J.J., and Cavada, B.S. (1997) The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett., 405, 114-118.
    • (1997) FEBS Lett. , vol.405 , pp. 114-118
    • Sanz-Aparicio, J.1    Hermoso, J.2    Grangeiro, T.B.3    Calvete, J.J.4    Cavada, B.S.5
  • 36
    • 0019889057 scopus 로고
    • Thermodynamics of concanavalin A dimer-tetramer self-association: Sedimentation equilibrium studies
    • Senear, D.F. and Teller, D.C. (1981) Thermodynamics of concanavalin A dimer-tetramer self-association: Sedimentation equilibrium studies. Biochemistry 20, 3076-3083.
    • (1981) Biochemistry , vol.20 , pp. 3076-3083
    • Senear, D.F.1    Teller, D.C.2
  • 37
    • 0031588904 scopus 로고    scopus 로고
    • Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity
    • Sharma, V. and Surolia, A. (1997) Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity. J. Mol. Biol., 267, 433-445.
    • (1997) J. Mol. Biol. , vol.267 , pp. 433-445
    • Sharma, V.1    Surolia, A.2
  • 38
    • 0025222989 scopus 로고
    • Legume lectins - A large family of homologous proteins
    • Sharon, N. and Lis, H. (1990) Legume lectins - a large family of homologous proteins. FASEB J., 4, 3198-3208.
    • (1990) FASEB J. , vol.4 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 39
    • 0035882421 scopus 로고    scopus 로고
    • Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization
    • Srinivas, V.R., Reddy, G.B., Ahmad, N., Swaminathan, C.P., Mitra, N., and Surolia, A. (2001) Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization. Biochim. Biophys. Acta, 1527, 102-111.
    • (2001) Biochim. Biophys. Acta , vol.1527 , pp. 102-111
    • Srinivas, V.R.1    Reddy, G.B.2    Ahmad, N.3    Swaminathan, C.P.4    Mitra, N.5    Surolia, A.6


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