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Volumn 359, Issue 2, 2007, Pages 221-226

Family 18 chitolectins: Comparison of MGP40 and HUMGP39

Author keywords

Binding; Chitinases; Mechanism; Oligosaccharide

Indexed keywords

CARBOHYDRATE; CHITIN; CHITOLECTIN; GLUTAMIC ACID; GLUTAMINE; GLYCOPROTEIN GP 39; GLYCOSIDASE; LECTIN; LEUCINE; LIGAND; MAMMARY GLAND PROTEIN 40; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 34250020788     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.05.074     Document Type: Article
Times cited : (21)

References (28)
  • 1
    • 0032714186 scopus 로고    scopus 로고
    • Physiological aspects of chitin catabolism in marine bacteria
    • Keyhani N.O., and Roseman S. Physiological aspects of chitin catabolism in marine bacteria. Biochim. Biophys. Acta 1473 (1999) 108-122
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 108-122
    • Keyhani, N.O.1    Roseman, S.2
  • 2
    • 0034506072 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics
    • Henrissat B., and Davies G.J. Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics. Plant Physiol. 124 (2000) 1515-1519
    • (2000) Plant Physiol. , vol.124 , pp. 1515-1519
    • Henrissat, B.1    Davies, G.J.2
  • 3
    • 0033288956 scopus 로고    scopus 로고
    • Function of chitin oligosaccharides in plant and animal development
    • Bakkers J., Kijne J.W., and Spaink H.P. Function of chitin oligosaccharides in plant and animal development. EXS 87 (1999) 71-83
    • (1999) EXS , vol.87 , pp. 71-83
    • Bakkers, J.1    Kijne, J.W.2    Spaink, H.P.3
  • 6
    • 0036297773 scopus 로고    scopus 로고
    • The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism
    • Bortone K., Monzingo A.F., Ernst S., and Robertus J.D. The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism. J. Mol. Biol. 320 (2002) 293-302
    • (2002) J. Mol. Biol. , vol.320 , pp. 293-302
    • Bortone, K.1    Monzingo, A.F.2    Ernst, S.3    Robertus, J.D.4
  • 7
    • 0037067670 scopus 로고    scopus 로고
    • Structure of human chiototriosidase. Implications for specific inhibitor design and function of mammalin chitnase-like lectins
    • Fusetti F., Moeller H.V., Houston D., Rozeboom H.J., Dijkstra B.W., Boot R.G., Aerts J.M., and van Aalten D.M. Structure of human chiototriosidase. Implications for specific inhibitor design and function of mammalin chitnase-like lectins. J. Biol. Chem. 277 (2002) 25537-25544
    • (2002) J. Biol. Chem. , vol.277 , pp. 25537-25544
    • Fusetti, F.1    Moeller, H.V.2    Houston, D.3    Rozeboom, H.J.4    Dijkstra, B.W.5    Boot, R.G.6    Aerts, J.M.7    van Aalten, D.M.8
  • 8
    • 0034064512 scopus 로고    scopus 로고
    • The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis
    • Hollis T., Monzingo A.F., Bortone K., Ernst S., Cox R., and Robertus J.D. The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis. Protein Sci. 9 (2000) 544-551
    • (2000) Protein Sci. , vol.9 , pp. 544-551
    • Hollis, T.1    Monzingo, A.F.2    Bortone, K.3    Ernst, S.4    Cox, R.5    Robertus, J.D.6
  • 9
    • 0043031435 scopus 로고    scopus 로고
    • Structure and ligand-induced conformational change of the 39 kDa glycoprotein from human articular chondrocytes
    • Houston D.R., Anneliese D.R., Joanne C.K., and van Aalten D.M. Structure and ligand-induced conformational change of the 39 kDa glycoprotein from human articular chondrocytes. J. Biol. Chem. 278 (2003) 30206-30212
    • (2003) J. Biol. Chem. , vol.278 , pp. 30206-30212
    • Houston, D.R.1    Anneliese, D.R.2    Joanne, C.K.3    van Aalten, D.M.4
  • 10
    • 0037113166 scopus 로고    scopus 로고
    • The cyclic dipeptide C1-4[cyclo-(l-Arg-d-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate
    • Houston D.R., Eggleston I., Synstad B., Eijsink V.G., and van Aalten D.M. The cyclic dipeptide C1-4[cyclo-(l-Arg-d-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate. Biochem. J. 368 (2002) 23-27
    • (2002) Biochem. J. , vol.368 , pp. 23-27
    • Houston, D.R.1    Eggleston, I.2    Synstad, B.3    Eijsink, V.G.4    van Aalten, D.M.5
  • 12
    • 0007151227 scopus 로고    scopus 로고
    • Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution
    • Matsumoto T., Nonaka T., Hashimoto M., Watanabe T., and Mitsui Y. Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution. Proc. Jpn. Acad. 75 (1999) 269-274
    • (1999) Proc. Jpn. Acad. , vol.75 , pp. 269-274
    • Matsumoto, T.1    Nonaka, T.2    Hashimoto, M.3    Watanabe, T.4    Mitsui, Y.5
  • 13
    • 0037312848 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7
    • Orikoshi H., Baba N., Nakayama S., Kashu H., Miyamoto K., Yasuda M., Inamori Y., and Tsujibo H. Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7. J. Bacteriol. 185 (2003) 1153-1160
    • (2003) J. Bacteriol. , vol.185 , pp. 1153-1160
    • Orikoshi, H.1    Baba, N.2    Nakayama, S.3    Kashu, H.4    Miyamoto, K.5    Yasuda, M.6    Inamori, Y.7    Tsujibo, H.8
  • 15
    • 0034647424 scopus 로고    scopus 로고
    • Structures of chitobiase mutants complexed with the substrate di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540
    • Prag G., Papanikolau Y., Tavlas G., Vorgias C.E., Petratos K., and Oppenheim A.B. Structures of chitobiase mutants complexed with the substrate di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J. Mol. Biol. 300 (2000) 611-617
    • (2000) J. Mol. Biol. , vol.300 , pp. 611-617
    • Prag, G.1    Papanikolau, Y.2    Tavlas, G.3    Vorgias, C.E.4    Petratos, K.5    Oppenheim, A.B.6
  • 16
    • 0032697044 scopus 로고    scopus 로고
    • Mutations of endo-beta-N-acetylglucoseaminidase H active site residue Asp 130 and Glu 132: activities and conformations
    • Rao V., Cui T., Guan C., and Roey P.V. Mutations of endo-beta-N-acetylglucoseaminidase H active site residue Asp 130 and Glu 132: activities and conformations. Protein Sci. 8 (1999) 2338-2346
    • (1999) Protein Sci. , vol.8 , pp. 2338-2346
    • Rao, V.1    Cui, T.2    Guan, C.3    Roey, P.V.4
  • 17
    • 0029644724 scopus 로고
    • Crystal structure of endo-beta-N-acetylglucoseaminidase H at 1.9 Å resolution: active-site geometry and substrate recognition
    • Rao V., Guan C., and Roey P.V. Crystal structure of endo-beta-N-acetylglucoseaminidase H at 1.9 Å resolution: active-site geometry and substrate recognition. Structure 3 (1995) 449-457
    • (1995) Structure , vol.3 , pp. 449-457
    • Rao, V.1    Guan, C.2    Roey, P.V.3
  • 18
    • 0035907391 scopus 로고    scopus 로고
    • The crystal structure of a novel mammalian lectin, Ym1, suggests a saccharide binding site
    • Sun Y.J., Chang N.C., Hung S.I., Chou C.C., and Hsiao C.D. The crystal structure of a novel mammalian lectin, Ym1, suggests a saccharide binding site. J. Biol. Chem. 276 (2001) 17507-17514
    • (2001) J. Biol. Chem. , vol.276 , pp. 17507-17514
    • Sun, Y.J.1    Chang, N.C.2    Hung, S.I.3    Chou, C.C.4    Hsiao, C.D.5
  • 19
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga A.C., Armand S., Kalk K.H., Isogai A., Henrissat B., and Dijkstra B.W. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34 (1995) 15619-15623
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 20
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with inhibitor
    • Terwisscha van Scheltinga A.C., Kalk K.H., Beintema J.J., and Dijkstra B.W. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with inhibitor. Structure 2 (1994) 181-1189
    • (1994) Structure , vol.2 , pp. 181-1189
    • Terwisscha van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 23
    • 0028170801 scopus 로고
    • Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate
    • Van Roey P., Rao V., Plummer Jr. T.H., and Tarentino A.L. Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate. Biochemistry 33 (1994) 13989-13996
    • (1994) Biochemistry , vol.33 , pp. 13989-13996
    • Van Roey, P.1    Rao, V.2    Plummer Jr., T.H.3    Tarentino, A.L.4
  • 24
    • 0037066770 scopus 로고    scopus 로고
    • Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster
    • Varela P.F., LIera A.S., Mariuzza R.A., and Tormo J. Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster. J. Biol. Chem. 277 (2002) 13229-13236
    • (2002) J. Biol. Chem. , vol.277 , pp. 13229-13236
    • Varela, P.F.1    LIera, A.S.2    Mariuzza, R.A.3    Tormo, J.4
  • 25
    • 0034636840 scopus 로고    scopus 로고
    • Structural basis for the substratespecificity of endo-beta-N-acetylglucoseaminidase F(3)
    • Waddling C.A., Plummer T.H.J., Tarentino A.L., and van Roey P. Structural basis for the substratespecificity of endo-beta-N-acetylglucoseaminidase F(3). Biochemistry 39 (2000) 7878-7885
    • (2000) Biochemistry , vol.39 , pp. 7878-7885
    • Waddling, C.A.1    Plummer, T.H.J.2    Tarentino, A.L.3    van Roey, P.4
  • 26
    • 0035815378 scopus 로고    scopus 로고
    • Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitine hydrolysis by Bacillus circulans chitinase A1
    • Watanabe T., Ishibashi A., Ariga Y., Yashimoto M., Nikaidou N., Sugiyama J., Matsumoto T., and Nonaka T. Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitine hydrolysis by Bacillus circulans chitinase A1. FEBS Lett. 494 (2001) 74-78
    • (2001) FEBS Lett. , vol.494 , pp. 74-78
    • Watanabe, T.1    Ishibashi, A.2    Ariga, Y.3    Yashimoto, M.4    Nikaidou, N.5    Sugiyama, J.6    Matsumoto, T.7    Nonaka, T.8
  • 27
    • 0141621106 scopus 로고    scopus 로고
    • Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39
    • Fusetti F., Pijning T., Kalk K.H., Bos E., and Dijkstra B.W. Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39. J. Biol. Chem. 278 (2003) 37753-37760
    • (2003) J. Biol. Chem. , vol.278 , pp. 37753-37760
    • Fusetti, F.1    Pijning, T.2    Kalk, K.H.3    Bos, E.4    Dijkstra, B.W.5
  • 28
    • 33947533891 scopus 로고    scopus 로고
    • Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides
    • Kumar J., Ethayathulla A.S., Srivastava D.B., Singh N., Sharma S., Kaur P., Srinivasan A., and Singh T.P. Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides. Acta Cryst. D 63 (2007) 437-446
    • (2007) Acta Cryst. D , vol.63 , pp. 437-446
    • Kumar, J.1    Ethayathulla, A.S.2    Srivastava, D.B.3    Singh, N.4    Sharma, S.5    Kaur, P.6    Srinivasan, A.7    Singh, T.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.