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Volumn 18, Issue 9, 1999, Pages 2313-2322

Tachylectin-2: Crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus

Author keywords

Animal lectin; Crystal structure; Horseshoe crab; N acetylglucosamine; propeller

Indexed keywords

CARBOHYDRATE; LECTIN; N ACETYLGLUCOSAMINE; POLYPEPTIDE; PROTEIN;

EID: 0033522446     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.9.2313     Document Type: Article
Times cited : (151)

References (42)
  • 3
    • 0030462561 scopus 로고    scopus 로고
    • Crystal structure of coagulogen, the clotting protein from horseshoe crab: A structural homologue of nerve growth factor
    • Bergner, A., Oganessyan, V., Muta, T., Iwanaga, S., Typke, D., Huber, R. and Bode, W. (1996) Crystal structure of coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor. EMBO J., 15, 6789-6797.
    • (1996) EMBO J. , vol.15 , pp. 6789-6797
    • Bergner, A.1    Oganessyan, V.2    Muta, T.3    Iwanaga, S.4    Typke, D.5    Huber, R.6    Bode, W.7
  • 4
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 5
    • 0030919276 scopus 로고    scopus 로고
    • Selective binding of W-acetylglucosamine to chicken hepatic lectin
    • Burrows, L., Iobst, S.T. and Drickamer, K. (1997) Selective binding of W-acetylglucosamine to chicken hepatic lectin. Biochem. J., 324, 673-680.
    • (1997) Biochem. J. , vol.324 , pp. 673-680
    • Burrows, L.1    Iobst, S.T.2    Drickamer, K.3
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 7
    • 0028813772 scopus 로고
    • 1.8 Å crystal structure of the C-terminal domain of rabbit serum haemopexin
    • Faber, H.R., Groom, C.R., Baker, H.M., Morgan, W.T., Smith, A. and Baker, E.N. (1995) 1.8 Å crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure, 3, 551-559.
    • (1995) Structure , vol.3 , pp. 551-559
    • Faber, H.R.1    Groom, C.R.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 8
    • 0029987839 scopus 로고    scopus 로고
    • The instructive role of innate immunity in the acquired immune response
    • Fearon, D.T. and Locksley, R.M. (1996) The instructive role of innate immunity in the acquired immune response. Science, 272, 50-54.
    • (1996) Science , vol.272 , pp. 50-54
    • Fearon, D.T.1    Locksley, R.M.2
  • 9
    • 0033524926 scopus 로고    scopus 로고
    • A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides
    • Inamori, K., Saito, T., Iwaki, D., Nagira, T., Iwanaga, S., Arisaka, F. and Kawabata, S. (1999) A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J. Biol. Chem., 274, 3272-3278.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3272-3278
    • Inamori, K.1    Saito, T.2    Iwaki, D.3    Nagira, T.4    Iwanaga, S.5    Arisaka, F.6    Kawabata, S.7
  • 11
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga, S., Kawabata, S. and Muta, T. (1998) New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem.. 123, 1-15.
    • (1998) J. Biochem.. , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 12
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T.A. (1978) A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr., 11, 268-272.
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, PJ. (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.J.1
  • 14
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • La Fortelle, E. de and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 15
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. and Wilson, K.S. (1993) Automated refinement of protein models. Acta Crystallogr., D49, 129-147.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 16
    • 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. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 17
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Oxford University Press, Oxford
    • Leslie, A.G.W. (1991) Molecular data processing. In Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Crystallographic Computing 5. Oxford University Press, Oxford, pp. 50-61.
    • (1991) Crystallographic Computing , vol.5 , pp. 50-61
    • Leslie, A.G.W.1
  • 18
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller
    • Li, J. et al. (1995) Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller. Structure, 3, 541-549.
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.1
  • 20
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol., 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 21
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R. and Janeway, C.A. (1997) Innate immunity: the virtues of a nonclonal system of recognition. Cell, 91, 295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 22
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 23
    • 0026671355 scopus 로고
    • Structural principles for the propeller assembly of β-sheets: The preference for seven-fold symmetry
    • Murzin, A.G. (1992) Structural principles for the propeller assembly of β-sheets: the preference for seven-fold symmetry. Proteins, 14, 191-201.
    • (1992) Proteins , vol.14 , pp. 191-201
    • Murzin, A.G.1
  • 24
    • 0028897416 scopus 로고
    • Purified horseshoe crab factor G. Reconstitution and characterization of the (1→3)-β-D-glucan-sensitive serine protease cascade
    • Muta, T., Seki, N., Takaki, Y., Hashimoto, R., Oda, T., Iwanaga A., Tokunaga, F. and Iwanaga, S. (1995) Purified horseshoe crab factor G. Reconstitution and characterization of the (1→3)-β-D-glucan-sensitive serine protease cascade. J. Biol. Chem., 270, 892-897.
    • (1995) J. Biol. Chem. , vol.270 , pp. 892-897
    • Muta, T.1    Seki, N.2    Takaki, Y.3    Hashimoto, R.4    Oda, T.5    Iwanaga, A.6    Tokunaga, F.7    Iwanaga, S.8
  • 26
    • 0017046962 scopus 로고
    • A clotlable protein (coagulogen) from amoebocyte lysate of japanese horseshoe crab (Tachypleus tridentatus)
    • Nakamura, S., Iwanaga, S., Harada, T. and Niwa, M. (1976) A clotlable protein (coagulogen) from amoebocyte lysate of japanese horseshoe crab (Tachypleus tridentatus). Its isolation and biochemical properties. J. Biochem., 80, 1011-1021.
    • (1976) Its Isolation and Biochemical Properties. J. Biochem. , vol.80 , pp. 1011-1021
    • Nakamura, S.1    Iwanaga, S.2    Harada, T.3    Niwa, M.4
  • 27
    • 0024076694 scopus 로고
    • Intracellular serine-protease zymogen, factor C, from horseshoe crab hemocytes. Its activation by synthetic lipid A analogues and acidic phospholipids
    • Nakamura, T., Tokunaga, F., Morita, T., Iwanaga, S., Kusumoto, S., Shiba, T., Kobayashi, T. and Inoue, K. (1988) Intracellular serine-protease zymogen, factor C, from horseshoe crab hemocytes. Its activation by synthetic lipid A analogues and acidic phospholipids. Eur. J. Biochem., 176, 89-94.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 89-94
    • Nakamura, T.1    Tokunaga, F.2    Morita, T.3    Iwanaga, S.4    Kusumoto, S.5    Shiba, T.6    Kobayashi, T.7    Inoue, K.8
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet., 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 29
    • 0029611240 scopus 로고
    • Purification, characterization and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes
    • Okino, N., Kawabata, S., Saito, T., Hirata, M., Takagi, T. and Iwanaga, S. (1995) Purification, characterization and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J. Biol. Chem., 270, 31008-31015.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31008-31015
    • Okino, N.1    Kawabata, S.2    Saito, T.3    Hirata, M.4    Takagi, T.5    Iwanaga, S.6
  • 31
    • 0025091235 scopus 로고
    • Occurence and structure of lipoteichoic acids in the genus Staphylococcus
    • Ruhland, G.J. and Fiedler, F. (1990) Occurence and structure of lipoteichoic acids in the genus Staphylococcus. Arch. Microbiol., 154, 375-379.
    • (1990) Arch. Microbiol. , vol.154 , pp. 375-379
    • Ruhland, G.J.1    Fiedler, F.2
  • 33
    • 0030662197 scopus 로고    scopus 로고
    • A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides
    • Saito, T., Kawabata, S., Hirata, M. and Iwanaga, S. (1997) A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J. Biol. Chem., 272, 30703-30708.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30703-30708
    • Saito, T.1    Kawabata, S.2    Hirata, M.3    Iwanaga, S.4
  • 34
    • 0000728003 scopus 로고
    • Tutorial on automated Patterson interpretation to find heavy atoms
    • Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Oxford University Press, Oxford
    • Sheldrick, G. (1991) Tutorial on automated Patterson interpretation to find heavy atoms. In Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Crystallographic Computing 5. Oxford University Press, Oxford, pp. 145-157.
    • (1991) Crystallographic Computing , vol.5 , pp. 145-157
    • Sheldrick, G.1
  • 35
    • 0027364986 scopus 로고
    • Limulus test for detecting bacterial endotoxins
    • Tanaka, S. and Iwanaga, S. (1993) Limulus test for detecting bacterial endotoxins. Methods Enzymol., 223, 358-364.
    • (1993) Methods Enzymol. , vol.223 , pp. 358-364
    • Tanaka, S.1    Iwanaga, S.2
  • 36
    • 0025989172 scopus 로고
    • Morphology of the granular hemocytes of the japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances
    • Toh, Y., Mizutani, A., Tokunaga, F. and Iwanaga, S. (1991) Morphology of the granular hemocytes of the japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances. Cell Tissue Res., 266, 137-147.
    • (1991) Cell Tissue Res. , vol.266 , pp. 137-147
    • Toh, Y.1    Mizutani, A.2    Tokunaga, F.3    Iwanaga, S.4
  • 37
    • 0030297443 scopus 로고    scopus 로고
    • Mannose-binding lectin: The pluripotent molecule of the innate immune system
    • Turner, M.W. (1996) Mannose-binding lectin: the pluripotent molecule of the innate immune system. Immunol. Today, 11, 532-540.
    • (1996) Immunol. Today , vol.11 , pp. 532-540
    • Turner, M.W.1
  • 38
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J. and Wiley, D.C. (1988) Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature, 333, 426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 39
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis, W.I. and Drickamer, K. (1994) Trimeric structure of a C-type mannose-binding protein. Structure, 2, 1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 40
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of the lectin-carbohydrate recognition
    • Weis, W.I. and Drickamer, K. (1996) Structural basis of the lectin-carbohydrate recognition. Annu. Rev. Biochem., 65, 441-473.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 41
    • 0025194445 scopus 로고
    • 2.2 Å resolution analysis of two refined N-acetyl-neuraminyl-lactose-wheat germ agglutinin isolectin complexes
    • Wright, C.S. (1990) 2.2 Å resolution analysis of two refined N-acetyl-neuraminyl-lactose-wheat germ agglutinin isolectin complexes. J. Mol. Biol., 215, 635-651.
    • (1990) J. Mol. Biol. , vol.215 , pp. 635-651
    • Wright, C.S.1
  • 42
    • 0026592054 scopus 로고
    • The three-dimensional structures of methanol dehydrogenases from two methylotrophic bacteria at 2.6 Å resolution
    • Xia, Z., Dai, W., Xiong, J. and Hao, Z. (1992) The three-dimensional structures of methanol dehydrogenases from two methylotrophic bacteria at 2.6 Å resolution. J. Biol. Chem., 267, 22289-22297.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22289-22297
    • Xia, Z.1    Dai, W.2    Xiong, J.3    Hao, Z.4


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