메뉴 건너뛰기




Volumn 90, Issue 9, 2006, Pages 1230-1237

Multivalency in lectins - A crystallographic, modelling and light-scattering study involving peanut lectin and a bivalent ligand

Author keywords

Crosslinking; Crystal structure prediction; Crystalline array; Lectin carbohydrate interactions; Ligand specificity

Indexed keywords

ARACHIS HYPOGAEA;

EID: 33744484324     PISSN: 00113891     EISSN: 00113891     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (31)
  • 1
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific proteins that mediate cellular recognition
    • Lis, H. and Sharon, N., Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem. Rev., 1998, 98, 637-674.
    • (1998) Chem. Rev. , vol.98 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 3
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris, R., Principles of structures of animal and plant lectins. Biochim. Biophys. Acta, 2002, 1572, 198-208.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 4
    • 33744480991 scopus 로고    scopus 로고
    • Lectin database available online
    • Bettler, H. M., Loris, R. and Imberty, A., Lectin database available online at http://cermav.cnrs.fr/lectines.
    • Bettler, H.M.1    Loris, R.2    Imberty, A.3
  • 5
    • 0037136412 scopus 로고    scopus 로고
    • Binding and crosslinking properties of galectin
    • Brewer, C. F., Binding and crosslinking properties of galectin. Biochim. Biophys. Acta, 2002, 1572, 255-262.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 255-262
    • Brewer, C.F.1
  • 6
    • 0029064070 scopus 로고
    • Multiplicity of lectin carbohydrate interactions
    • Drickamer, K.. Multiplicity of lectin carbohydrate interactions. Nature Struct. Biol., 1995, 2, 437-439.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 437-439
    • Drickamer, K.1
  • 7
    • 0001484582 scopus 로고    scopus 로고
    • Multivalent lectin-carbohydrate crosslinking interactions
    • Brewer, C. F., Multivalent lectin-carbohydrate crosslinking interactions. Chemtracts Biochem. Mol. Biol., 1996, 6, 165-179.
    • (1996) Chemtracts Biochem. Mol. Biol. , vol.6 , pp. 165-179
    • Brewer, C.F.1
  • 8
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer, C. F., Miceli, M. C. and Baum, L. G., Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol., 2002, 12, 616-623.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 9
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W. I., Drickamer, K. and Hendrickson, W. A., Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature, 1992, 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 10
    • 0028676128 scopus 로고
    • Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides
    • Bourne, Y. et al., Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nature Struct. Biol., 1994, 1, 863-870.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 863-870
    • Bourne, Y.1
  • 11
    • 0030720932 scopus 로고    scopus 로고
    • X-ray crystallographic studies of unique crosslinked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin
    • Olsen, L. R., Dessen, A., Gupta, D., Sabesan, S., Sacchettini, J. and Brewer, C. F., X-ray crystallographic studies of unique crosslinked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin. Biochemistry, 1997, 36, 15073-15080.
    • (1997) Biochemistry , vol.36 , pp. 15073-15080
    • Olsen, L.R.1    Dessen, A.2    Gupta, D.3    Sabesan, S.4    Sacchettini, J.5    Brewer, C.F.6
  • 12
    • 0035852973 scopus 로고    scopus 로고
    • Multivalent protein-carbohydrate interactions. A new paradigm for supermolecular assembly and signal transduction
    • Sacchettini, J. C., Baum, L. G. and Brewer, C. F., Multivalent protein-carbohydrate interactions. A new paradigm for supermolecular assembly and signal transduction. Biochemistry, 2001, 40, 3009-3015.
    • (2001) Biochemistry , vol.40 , pp. 3009-3015
    • Sacchettini, J.C.1    Baum, L.G.2    Brewer, C.F.3
  • 13
    • 0029658497 scopus 로고    scopus 로고
    • The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentose: Evidence for two unique binding modes
    • Wright, C. S. and Hester, G., The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentose: evidence for two unique binding modes. Structure, 1996, 4, 1339-1352.
    • (1996) Structure , vol.4 , pp. 1339-1352
    • Wright, C.S.1    Hester, G.2
  • 14
    • 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., The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: Crystal structure of cross-linked FRIL. J. Mol. Biol., 2000, 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
  • 15
    • 0242693280 scopus 로고    scopus 로고
    • Computational analysis of multivalency in lectin structures of garlic lectin-oligosaccharide complexes and their aggregates
    • Ramachandraiah, G., Chandra, N. R., Surolia, A. and Vijayan, M., Computational analysis of multivalency in lectin structures of garlic lectin-oligosaccharide complexes and their aggregates. Glycobiology, 2003, 13, 765-775.
    • (2003) Glycobiology , vol.13 , pp. 765-775
    • Ramachandraiah, G.1    Chandra, N.R.2    Surolia, A.3    Vijayan, M.4
  • 16
    • 0029997826 scopus 로고    scopus 로고
    • Conformation of 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. and Vijayan, M., Conformation of protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex. J. Mol. Biol., 1996, 256, 281-296.
    • (1996) J. Mol. Biol. , vol.256 , pp. 281-296
    • Banerjee, R.1    Das, K.2    Ravishankar, R.3    Suguna, K.4    Surolia, A.5    Vijayan, M.6
  • 17
    • 0000492269 scopus 로고    scopus 로고
    • Crystal structure of the peanut lectin-T-antigen complex. Carbohydrate specificity generated by water bridges
    • Ravishankar, R., Ravindran, M., Suguna, K., Surolia, A. and Vijayan, M., Crystal structure of the peanut lectin-T-antigen complex. Carbohydrate specificity generated by water bridges. Curr. Sci., 1997, 72, 855-861.
    • (1997) Curr. Sci. , vol.72 , pp. 855-861
    • Ravishankar, R.1    Ravindran, M.2    Suguna, K.3    Surolia, A.4    Vijayan, M.5
  • 18
    • 0033180444 scopus 로고    scopus 로고
    • Structure of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNac specific legume lectins
    • Ravishankar, R., Suguna, K., Surolia, A. and Vijayan, M., Structure of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNac specific legume lectins. Acta Crystallogr. Sect. D, 1999, 55, 1375-1382.
    • (1999) Acta Crystallogr. Sect. D , vol.55 , pp. 1375-1382
    • Ravishankar, R.1    Suguna, K.2    Surolia, A.3    Vijayan, M.4
  • 19
    • 0035874139 scopus 로고    scopus 로고
    • Crystal structures of the peanut lectin-lactose complex at acidic pH: Retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site
    • Ravishankar, R., Thomas, C. J., Suguna, K., Surolia, A. and Vijayan, M., Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site. Proteins, 2001, 43, 260-270.
    • (2001) Proteins , vol.43 , pp. 260-270
    • Ravishankar, R.1    Thomas, C.J.2    Suguna, K.3    Surolia, A.4    Vijayan, M.5
  • 20
  • 21
    • 0037070633 scopus 로고    scopus 로고
    • Photoswitchable multivalent sugar ligands: Synthesis, isomerization, and lectin binding studies of azobenzene-glycopyranoside derivatives
    • Srinivas, O., Mitra, N., Surolia, A. and Jayaraman, N., Photoswitchable multivalent sugar ligands: synthesis, isomerization, and lectin binding studies of azobenzene-glycopyranoside derivatives. J. Am. Chem. Soc., 2002, 124, 2124-2125.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2124-2125
    • Srinivas, O.1    Mitra, N.2    Surolia, A.3    Jayaraman, N.4
  • 22
    • 24044434625 scopus 로고    scopus 로고
    • Photoswitchable cluster glycosides as tools to probe carbohydrate-protein interactions: Synthesis and lectin-binding studies of azobenzene containing multivalent sugar ligands
    • Srinivas, O., Mitra, N., Surolia, A. and Jayaraman, N., Photoswitchable cluster glycosides as tools to probe carbohydrate-protein interactions: synthesis and lectin-binding studies of azobenzene containing multivalent sugar ligands. Glycobiology, 2005, 15, 861-873.
    • (2005) Glycobiology , vol.15 , pp. 861-873
    • Srinivas, O.1    Mitra, N.2    Surolia, A.3    Jayaraman, N.4
  • 24
    • 0028103275 scopus 로고
    • CCP4 (Collaborative Computational Project, No. 4)
    • CCP4 (Collaborative Computational Project, No. 4). Acta Crystallogr. Sect. D, 1994, 50, 760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 25
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, AMoRe: an automated package for molecular replacement. Acta Crystallogr. Sect. A, 1994, 50, 157-163.
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navaza1
  • 26
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen, G. E., ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr., 1997, 30, 1160-1161.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 27
    • 13544251502 scopus 로고    scopus 로고
    • The case for open-source software in drug discovery
    • DeLano, L. W., The case for open-source software in drug discovery. Drug Discovery Today, 2005, 10, 213-217.
    • (2005) Drug Discovery Today , vol.10 , pp. 213-217
    • DeLano, L.W.1
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 1991, 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0141918780 scopus 로고    scopus 로고
    • Complementary approaches to structure determination of icosahedral viruses
    • Lee, K. K. and Johnson, J. E., Complementary approaches to structure determination of icosahedral viruses. Curr. Opin. Struct. Biol., 2003, 13, 558-569.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 558-569
    • Lee, K.K.1    Johnson, J.E.2
  • 30
    • 4744344736 scopus 로고    scopus 로고
    • Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs
    • Orlova, E. V. and Saibil, H. R., Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs. Curr. Opin. Struct. Biol., 2004, 14, 584-590.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 584-590
    • Orlova, E.V.1    Saibil, H.R.2
  • 31
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H. M. et al., The protein data bank. Nucleic Acids Res., 2000, 28, 235-242.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.