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Volumn 23, Issue 7, 2013, Pages 797-805

Structural basis of preferential binding of fucose-containing saccharide by the Caenorhabditis elegans galectin LEC-6

Author keywords

Caenorhabditis elegans; crystal structure; frontal affinity chromatography; galactose 1 4 fucose; galectin

Indexed keywords

CAENORHABDITIS ELEGANS PROTEIN; DIMER; DISACCHARIDE; FUCOSE; GALACTOSE; GALECTIN; GLUTAMIC ACID; LEC 6 PROTEIN; MONOMER; MUTANT PROTEIN; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 84879884305     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt017     Document Type: Article
Times cited : (11)

References (55)
  • 2
    • 0030758114 scopus 로고    scopus 로고
    • The two lectin domains of the tandemrepeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties
    • Arata Y, Hirabayashi J, Kasai K. 1997. The two lectin domains of the tandemrepeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties. Studies with recombinant protein. J Biochem. 121:1002-1009.
    • (1997) Studies with Recombinant Protein. J Biochem. , vol.121 , pp. 1002-1009
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 5
    • 0034284122 scopus 로고    scopus 로고
    • Recent changes to RasMol, recombining the variants
    • Bernstein HJ. 2000. Recent changes to RasMol, recombining the variants. Trends Biochem Sci. 25:453-455.
    • (2000) Trends Biochem Sci. , vol.25 , pp. 453-455
    • Bernstein, H.J.1
  • 6
    • 0032825315 scopus 로고    scopus 로고
    • SWEET-WWW-based rapid 3D construction of oligo- and polysaccharides
    • Bohne A, Lang E, von der Lieth CW. 1999. SWEET-WWW-based rapid 3D construction of oligo- and polysaccharides. Bioinformatics. 15:767-768.
    • (1999) Bioinformatics. , vol.15 , pp. 767-768
    • Bohne, A.1    Lang, E.2    Von Der Lieth, C.W.3
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D. 50:760-763.
    • (1994) Acta Crystallogr D. , vol.50 , pp. 760-763
  • 11
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper DN. 2002. Galectinomics: Finding themes in complexity. Biochim Biophys Acta. 1572:209-231.
    • (2002) Biochim Biophys Acta. , vol.1572 , pp. 209-231
    • Cooper, D.N.1
  • 16
    • 33748370297 scopus 로고    scopus 로고
    • Development of an automated large-scale protein-crystallization and monitoring system for highthroughput protein-structure analyses
    • Hiraki M, Kato R, Nagai M, Satoh T, Hirano S, Ihara K, Kudo N, Nagae M, Kobayashi M, Inoue M, et al. 2006. Development of an automated large-scale protein-crystallization and monitoring system for highthroughput protein-structure analyses. Acta Crystallogr D. 62:1058-1065.
    • (2006) Acta Crystallogr D. , vol.62 , pp. 1058-1065
    • Hiraki, M.1    Kato, R.2    Nagai, M.3    Satoh, T.4    Hirano, S.5    Ihara, K.6    Kudo, N.7    Nagae, M.8    Kobayashi, M.9    Inoue, M.10
  • 17
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P. 2010. Dali server: Conservation mapping in 3D. Nucleic Acids Res. 38:W545-W549.
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 18
    • 70350400858 scopus 로고    scopus 로고
    • A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection
    • Ideo H, Fukushima K, Gengyo-Ando K, Mitani S, Dejima K, Nomura K, Yamashita K. 2009. A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. J Biol Chem. 284:26493-26501.
    • (2009) J Biol Chem. , vol.284 , pp. 26493-26501
    • Ideo, H.1    Fukushima, K.2    Gengyo-Ando, K.3    Mitani, S.4    Dejima, K.5    Nomura, K.6    Yamashita, K.7
  • 19
    • 79953197242 scopus 로고    scopus 로고
    • Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans
    • Ideo H, Matsuzaka T, Nonaka T, Seko A, Yamashita K. 2011. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. JBiol Chem. 286:11346-11355.
    • (2011) JBiol Chem. , vol.286 , pp. 11346-11355
    • Ideo, H.1    Matsuzaka, T.2    Nonaka, T.3    Seko, A.4    Yamashita, K.5
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers. , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 24
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • Kasai K, Hirabayashi J. 1996. Galectins: A family of animal lectins that decipher glycocodes. J Biochem. 119:1-8.
    • (1996) J Biochem. , vol.119 , pp. 1-8
    • Kasai, K.1    Hirabayashi, J.2
  • 25
    • 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 Crystallogr. 24:946-950.
    • (1991) J Appl Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 26
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. 2007. Inference of macromolecular assemblies from crystalline state. J Mol Biol. 372:774-797.
    • (2007) J Mol Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 27
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A. 2008. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc. 3:1171-1179.
    • (2008) Nat Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 29
    • 77955352019 scopus 로고    scopus 로고
    • MSAProbs: Multiple sequence alignment based on pair hidden Markov models and partition function posterior probabilities
    • Liu Y, Schmidt B, Maskell DL. 2010. MSAProbs: Multiple sequence alignment based on pair hidden Markov models and partition function posterior probabilities. Bioinformatics. 26:1958-1964.
    • (2010) Bioinformatics. , vol.26 , pp. 1958-1964
    • Liu, Y.1    Schmidt, B.2    Maskell, D.L.3
  • 30
    • 79952996100 scopus 로고    scopus 로고
    • Caenorhabditis elegans galectins LEC-6 and LEC-10 interact with similar glycoconjugates in the intestine
    • Maduzia LL, Yu E, Zhang Y. 2011. Caenorhabditis elegans galectins LEC-6 and LEC-10 interact with similar glycoconjugates in the intestine. J Biol Chem. 286:4371-4381.
    • (2011) J Biol Chem. , vol.286 , pp. 4371-4381
    • Maduzia, L.L.1    Yu, E.2    Zhang, Y.3
  • 32
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ. 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 34
    • 33845987092 scopus 로고    scopus 로고
    • Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition
    • Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R. 2006. Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition. J Biol Chem. 281:35884-35893.
    • (2006) J Biol Chem. , vol.281 , pp. 35884-35893
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6    Kato, R.7
  • 35
    • 36348976981 scopus 로고    scopus 로고
    • Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue
    • Nagae M, Nishi N, Nakamura-Tsuruta S, Hirabayashi J, Wakatsuki S, Kato R. 2008. Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue. J Mol Biol. 375:119-135.
    • (2008) J Mol Biol. , vol.375 , pp. 119-135
    • Nagae, M.1    Nishi, N.2    Nakamura-Tsuruta, S.3    Hirabayashi, J.4    Wakatsuki, S.5    Kato, R.6
  • 38
    • 77950796599 scopus 로고    scopus 로고
    • Synthesis of fluorescence-labeled Galbeta1-3Fuc and Galbeta1-4Fuc as probes for the endogenous glyco-epitope recognized by galectins in Caenorhabditis elegans
    • Nishiyama K, Yamada A, Takahashi M, Takeuchi T, Kasai K, Kobayashi S, Natsugari H, Takahashi H. 2010. Synthesis of fluorescence-labeled Galbeta1-3Fuc and Galbeta1-4Fuc as probes for the endogenous glyco-epitope recognized by galectins in Caenorhabditis elegans. Chem Pharm Bull. 58:495-500.
    • (2010) Chem Pharm Bull. , vol.58 , pp. 495-500
    • Nishiyama, K.1    Yamada, A.2    Takahashi, M.3    Takeuchi, T.4    Kasai, K.5    Kobayashi, S.6    Natsugari, H.7    Takahashi, H.8
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, Carter CW, Jr. 1997. Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr A. 276:307-326.
    • (1997) Macromol Crystallogr A. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter Jr., C.W.3
  • 41
    • 79958081552 scopus 로고    scopus 로고
    • Presence of galactosylated core fucose on N-glycans in the planaria Dugesia japonica
    • Paschinger K, Razzazi-Fazeli E, Furukawa K, Wilson IB. 2011. Presence of galactosylated core fucose on N-glycans in the planaria Dugesia japonica. J Mass Spectrom. 46:561-567.
    • (2011) J Mass Spectrom. , vol.46 , pp. 561-567
    • Paschinger, K.1    Razzazi-Fazeli, E.2    Furukawa, K.3    Wilson, I.B.4
  • 44
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for highthroughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM. 2004. PRODRG: A tool for highthroughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr. 60:1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr. , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 46
    • 54549113417 scopus 로고    scopus 로고
    • Caenorhabditis elegans N-glycans containing a Gal-Fuc disaccharide unit linked to the innermost GlcNAc residue are recognized by C. Elegans galectin LEC-6
    • Takeuchi T, Hayama K, Hirabayashi J, Kasai K. 2008. Caenorhabditis elegans N-glycans containing a Gal-Fuc disaccharide unit linked to the innermost GlcNAc residue are recognized by C. elegans galectin LEC-6. Glycobiology. 18:882-890.
    • (2008) Glycobiology. , vol.18 , pp. 882-890
    • Takeuchi, T.1    Hayama, K.2    Hirabayashi, J.3    Kasai, K.4
  • 47
    • 71049177754 scopus 로고    scopus 로고
    • Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galbeta1- 4Fuc disaccharide unit which is present in Protostomia glycoconjugates
    • Takeuchi T, Nishiyama K, Sugiura K, Takahashi M, Yamada A, Kobayashi S, Takahashi H, Natsugari H, Kasai K. 2009. Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galbeta1- 4Fuc disaccharide unit which is present in Protostomia glycoconjugates. Glycobiology. 19:1503-1510.
    • (2009) Glycobiology. , vol.19 , pp. 1503-1510
    • Takeuchi, T.1    Nishiyama, K.2    Sugiura, K.3    Takahashi, M.4    Yamada, A.5    Kobayashi, S.6    Takahashi, H.7    Natsugari, H.8    Kasai, K.9
  • 49
    • 79960326428 scopus 로고    scopus 로고
    • Sugar-binding properties of the two lectin domains of LEC-1 with respect to the Galbeta1-4Fuc disaccharide unit present in protostomia glycoconjugates
    • Takeuchi T, Sugiura K, Nishiyama K, Takahashi H, Natsugari H, Arata Y, Kasai K. 2011. Sugar-binding properties of the two lectin domains of LEC-1 with respect to the Galbeta1-4Fuc disaccharide unit present in protostomia glycoconjugates. Biol Pharm Bull. 34:1134-1138.
    • (2011) Biol Pharm Bull. , vol.34 , pp. 1134-1138
    • Takeuchi, T.1    Sugiura, K.2    Nishiyama, K.3    Takahashi, H.4    Natsugari, H.5    Arata, Y.6    Kasai, K.7
  • 50
    • 58149343579 scopus 로고    scopus 로고
    • Glycobiology on the fly: Developmental and mechanistic insights from Drosophila
    • ten Hagen KG, Zhang L, Tian E, Zhang Y. 2009. Glycobiology on the fly: Developmental and mechanistic insights from Drosophila. Glycobiology. 19:102-111.
    • (2009) Glycobiology. , vol.19 , pp. 102-111
    • Ten Hagen, K.G.1    Zhang, L.2    Tian, E.3    Zhang, Y.4
  • 51
    • 73649148725 scopus 로고    scopus 로고
    • Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4- galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family
    • Titz A, Butschi A, Henrissat B, Fan YY, Hennet T, Razzazi-Fazeli E, Hengartner MO, Wilson IB, Kunzler M, Aebi M. 2009. Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4- galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family. J Biol Chem. 284:36223-36233.
    • (2009) J Biol Chem. , vol.284 , pp. 36223-36233
    • Titz, A.1    Butschi, A.2    Henrissat, B.3    Fan, Y.Y.4    Hennet, T.5    Razzazi-Fazeli, E.6    Hengartner, M.O.7    Wilson, I.B.8    Kunzler, M.9    Aebi, M.10
  • 52
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 53
    • 1642383648 scopus 로고    scopus 로고
    • A novel Gal(beta1-4)Gal(beta1-4)Fuc(alpha1-6)-core modification attached to the proximal N-acetylglucosamine of keyhole limpet haemocyanin (KLH) N-glycans
    • Wuhrer M, Robijn ML, Koeleman CA, Balog CI, Geyer R, Deelder AM, Hokke CH. 2004. A novel Gal(beta1-4)Gal(beta1-4)Fuc(alpha1-6)-core modification attached to the proximal N-acetylglucosamine of keyhole limpet haemocyanin (KLH) N-glycans. Biochem J. 378:625-632.
    • (2004) Biochem J. , vol.378 , pp. 625-632
    • Wuhrer, M.1    Robijn, M.L.2    Koeleman, C.A.3    Balog, C.I.4    Geyer, R.5    Deelder, A.M.6    Hokke, C.H.7
  • 55
    • 0031459388 scopus 로고    scopus 로고
    • A novel monoantennary complex-type sugar chain found in octopus rhodopsin: Occurrence of the Gal beta1->4Fuc group linked to the proximal N-acetylglucosamine residue of the trimannosyl core
    • Zhang Y, Iwasa T, Tsuda M, Kobata A, Takasaki S. 1997. A novel monoantennary complex-type sugar chain found in octopus rhodopsin: Occurrence of the Gal beta1->4Fuc group linked to the proximal N-acetylglucosamine residue of the trimannosyl core. Glycobiology. 7:1153-1158.
    • (1997) Glycobiology. , vol.7 , pp. 1153-1158
    • Zhang, Y.1    Iwasa, T.2    Tsuda, M.3    Kobata, A.4    Takasaki, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.