메뉴 건너뛰기




Volumn 14, Issue 10, 2004, Pages 923-929

Crystal structures of Erythrina cristagalli lectin with bound N-linked oligosaccharide and lactose

Author keywords

Crystal structure; Erythrina corallodendron lectin; Erythrina cristagalli lectin; N glycosylation; Protein carbohydrate interaction

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; ERYTHRINA EXTRACT; GLUTAMINE; GLYCINE; LACTOSE; LEUCINE; OLIGOSACCHARIDE; PLANT LECTIN;

EID: 4644263759     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwh114     Document Type: Article
Times cited : (44)

References (22)
  • 1
    • 0026170573 scopus 로고
    • The glycosylation of glycoprotein lectins. Intra- and inter-genus variation in N-linked oligosaccharide expression
    • Ashford, D.A., Dwek, R.A., Rademacher, T.W., Lis, H., and Sharon, N. (1991) The glycosylation of glycoprotein lectins. Intra- and inter-genus variation in N-linked oligosaccharide expression. Carbohydrate Res., 213, 215-227.
    • (1991) Carbohydrate Res. , vol.213 , pp. 215-227
    • Ashford, D.A.1    Dwek, R.A.2    Rademacher, T.W.3    Lis, H.4    Sharon, N.5
  • 4
    • 0037144403 scopus 로고    scopus 로고
    • Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin
    • and others
    • Duggan, M.J., Quinn, C.P., Chaddock, J.A., Purkiss, J.R., Alexander, F.C.G., Doward, S., Fooks, S.J., Friis, L.M., Hall, Y.H.J., Kirby, E.R., and others. (2002) Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin. J. Biol. Chem., 277, 34846-34852.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34846-34852
    • Duggan, M.J.1    Quinn, C.P.2    Chaddock, J.A.3    Purkiss, J.R.4    Alexander, F.C.G.5    Doward, S.6    Fooks, S.J.7    Friis, L.M.8    Hall, Y.H.J.9    Kirby, E.R.10
  • 5
    • 0032502896 scopus 로고    scopus 로고
    • Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides
    • Elgavish, S. and Shaanan, B. (1998) Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides. J. Mol. Biol, 277, 917-932.
    • (1998) J. Mol. Biol. , vol.277 , pp. 917-932
    • Elgavish, S.1    Shaanan, B.2
  • 6
    • 0035085861 scopus 로고    scopus 로고
    • Chemical characteristics of dimer interfaces in the legume lectin family
    • Elgavish, S. and Shaanan, B. (2001) Chemical characteristics of dimer interfaces in the legume lectin family. Prot. Sci., 10, 753-761.
    • (2001) Prot. Sci. , vol.10 , pp. 753-761
    • Elgavish, S.1    Shaanan, B.2
  • 8
    • 0020122741 scopus 로고
    • Purification and properties of a D-galactose/N-acetyl-D-galactosamine-specitic lectin from Erythrina cristagalli
    • Iglesias, J. L., Lis, H., and Sharon, N. (1982) Purification and properties of a D-galactose/N-acetyl-D-galactosamine-specitic lectin from Erythrina cristagalli. Eur. J. Biochem., 123, 247-252.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 247-252
    • Iglesias, J.L.1    Lis, H.2    Sharon, N.3
  • 9
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • Kleywegt, G. and Jones, T.A. (1998) Databases in protein crystallography. Acta Crystallogr., D54, 1119-1131.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 1119-1131
    • Kleywegt, G.1    Jones, T.A.2
  • 10
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst., 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 11
    • 0035667291 scopus 로고    scopus 로고
    • Signature of quarternary structure in the sequences of legume lectins
    • Manoj, N. and Suguna, K. (2001) Signature of quarternary structure in the sequences of legume lectins. Protein Eng., 14, 735-745.
    • (2001) Protein Eng. , vol.14 , pp. 735-745
    • Manoj, N.1    Suguna, K.2
  • 12
    • 0030936959 scopus 로고    scopus 로고
    • Redefinition of the carbohydrate specificity of Erythrina corallodendron lectin based on solid-phase binding assays and molecular modeling of native and recombinant forms obtained by site-directed mutagenesis
    • Moreno, E., Teneberg, S., Adar, R., Sharon, N., Karlsson, K.A., and Angstrom, J. (1997) Redefinition of the carbohydrate specificity of Erythrina corallodendron lectin based on solid-phase binding assays and molecular modeling of native and recombinant forms obtained by site-directed mutagenesis. Biochemistry, 36, 4429-4437.
    • (1997) Biochemistry , vol.36 , pp. 4429-4437
    • Moreno, E.1    Teneberg, S.2    Adar, R.3    Sharon, N.4    Karlsson, K.A.5    Angstrom, J.6
  • 13
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza,, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr., A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 14
    • 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
  • 15
    • 0032489360 scopus 로고    scopus 로고
    • Carbohydrate specificity and quarternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution
    • Prabu, M.M., Sankaranarayanan, R., Puri, K.D., Sharma, V., Surolia, A., Vijayan, M., and Suguna, K. (1998) Carbohydrate specificity and quarternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution. J. Mol. Biol, 276, 787-796.
    • (1998) J. Mol. Biol. , vol.276 , pp. 787-796
    • Prabu, M.M.1    Sankaranarayanan, R.2    Puri, K.D.3    Sharma, V.4    Surolia, A.5    Vijayan, M.6    Suguna, K.7
  • 16
    • 0033120809 scopus 로고    scopus 로고
    • Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins
    • Prabu, M.M., Suguna, K., and Vijayan, M. (1999) Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins. Prot. Struct. Funct. Genet., 35, 58-69.
    • (1999) Prot. Struct. Funct. Genet. , vol.35 , pp. 58-69
    • Prabu, M.M.1    Suguna, K.2    Vijayan, M.3
  • 17
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan, B., Lis, H., and 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
  • 18
    • 0035882421 scopus 로고    scopus 로고
    • Legume lectin family, the "natural mutants of the quarternary 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 quarternary 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
  • 19
    • 0041568571 scopus 로고    scopus 로고
    • Isolation of the gene and large scale expression and purification of recombinant Erythrina cristagalli lectin
    • Stancombe, P.R., Alexander, F.C.G., Ling, R., Matheson, M., Shone, C.C., and Chaddock, J.A. (2003) Isolation of the gene and large scale expression and purification of recombinant Erythrina cristagalli lectin. Protein Exp. Purif., 30, 283-292.
    • (2003) Protein Exp. Purif. , vol.30 , pp. 283-292
    • Stancombe, P.R.1    Alexander, F.C.G.2    Ling, R.3    Matheson, M.4    Shone, C.C.5    Chaddock, J.A.6
  • 20
    • 0029929718 scopus 로고    scopus 로고
    • Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin
    • Surolia, A., Sharon, N., and Schwarz, F.P. (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
  • 21
    • 0036353416 scopus 로고    scopus 로고
    • High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-alpha-L-fucosyllactose and correlation with thermodynamic binding data
    • Svensson, C., Teneberg, S., Nilsson, C.L., Kjellberg, A., Schwarz, F.P., Sharon, N., and Krengel, U. (2002) High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-alpha-L-fucosyllactose and correlation with thermodynamic binding data. J. Mol. Biol., 32, 69-83.
    • (2002) J. Mol. Biol. , vol.32 , pp. 69-83
    • Svensson, C.1    Teneberg, S.2    Nilsson, C.L.3    Kjellberg, A.4    Schwarz, F.P.5    Sharon, N.6    Krengel, U.7
  • 22
    • 0028176447 scopus 로고
    • Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk
    • Teneberg, S., Angstrom, J., Jovall, P.A., and Karlsson, K.A. (1994) Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk. J. Biol. Chem., 269, 8554-8563.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8554-8563
    • Teneberg, S.1    Angstrom, J.2    Jovall, P.A.3    Karlsson, K.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.