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Volumn 158, Issue 3, 2007, Pages 255-266

Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): Crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides

Author keywords

Chito oligosaccharides; Dry secretion; Protein binding; Secretory glycoprotein; Sugar binding

Indexed keywords

CARBOHYDRATE; CHITINASE; GLYCOPROTEIN; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; PROTEIN; PROTEIN SPX 40; SECRETORY GLYCOPROTEIN 40; UNCLASSIFIED DRUG;

EID: 34248583798     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.11.002     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 0345688117 scopus 로고    scopus 로고
    • Family 18 chitinase oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A
    • Aronson N.N., Halloran B.A., Alexyev M.F., Amable L., Madura J.D., Pasupulati L., Worth C., and Roey P.V. Family 18 chitinase oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A. Biochem. J. 376 (2003) 87-95
    • (2003) Biochem. J. , vol.376 , pp. 87-95
    • Aronson, N.N.1    Halloran, B.A.2    Alexyev, M.F.3    Amable, L.4    Madura, J.D.5    Pasupulati, L.6    Worth, C.7    Roey, P.V.8
  • 2
    • 0032016637 scopus 로고    scopus 로고
    • Peptides generated from milk proteins in the bovine mammary gland during involution
    • Aslam M., and Hurley W.L. Peptides generated from milk proteins in the bovine mammary gland during involution. J. Dairy Sci. 81 (1997) 748-755
    • (1997) J. Dairy Sci. , vol.81 , pp. 748-755
    • Aslam, M.1    Hurley, W.L.2
  • 4
    • 0034664979 scopus 로고    scopus 로고
    • A novel mechanism of xylan binding by a lectin-like module from Streptomyces lividans xylanase 10A
    • Boraston A.B., Tomme P., Amandoron E.A., and Kilburn D.G. A novel mechanism of xylan binding by a lectin-like module from Streptomyces lividans xylanase 10A. Biochem. J. 350 (2000) 933-941
    • (2000) Biochem. J. , vol.350 , pp. 933-941
    • Boraston, A.B.1    Tomme, P.2    Amandoron, E.A.3    Kilburn, D.G.4
  • 6
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson S.K., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321 (1997) 557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, S.K.2    Henrissat, B.3
  • 7
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • Eftink M.R. Fluorescence methods for studying equilibrium macromolecule-ligand interactions. Methods Enzymol. 278 (1997) 221-257
    • (1997) Methods Enzymol. , vol.278 , pp. 221-257
    • Eftink, M.R.1
  • 8
    • 0029245824 scopus 로고
    • Inhibition of the proteinase activity in mastitic milk
    • Fang W., and Sandholm M. Inhibition of the proteinase activity in mastitic milk. J. Dairy Res. 62 (1995) 61-68
    • (1995) J. Dairy Res. , vol.62 , pp. 61-68
    • Fang, W.1    Sandholm, M.2
  • 9
    • 0035957051 scopus 로고    scopus 로고
    • Kinetic properties of chitinase-1 from fungal pathogen Coccidioides immitis
    • Fukamizo T., Saski C., Schelp E., Bortone K., and Robertus J.D. Kinetic properties of chitinase-1 from fungal pathogen Coccidioides immitis. Biochemistry 40 (2001) 2448-2454
    • (2001) Biochemistry , vol.40 , pp. 2448-2454
    • Fukamizo, T.1    Saski, C.2    Schelp, E.3    Bortone, K.4    Robertus, J.D.5
  • 10
    • 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
  • 11
  • 12
    • 0027505001 scopus 로고
    • Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family
    • Hakala B.E., White C., and Recklies A.D. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J. Biol. Chem. 268 (1993) 25803-25810
    • (1993) J. Biol. Chem. , vol.268 , pp. 25803-25810
    • Hakala, B.E.1    White, C.2    Recklies, A.D.3
  • 13
    • 0043031435 scopus 로고    scopus 로고
    • Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes
    • Houston D.R., Recklies A.D., Krupa J.C., 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    Recklies, A.D.2    Krupa, J.C.3    van Aalten, D.M.4
  • 14
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse M., Chen Y.G., Massague J., and Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell 96 (1999) 425-436
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 15
    • 0028788067 scopus 로고
    • Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drug FK506 (tacrolimus)
    • Itoh S., and Navia M.A. Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drug FK506 (tacrolimus). Protein Sci. 11 (1995) 2261-2268
    • (1995) Protein Sci. , vol.11 , pp. 2261-2268
    • Itoh, S.1    Navia, M.A.2
  • 16
    • 0003016299 scopus 로고
    • Crystallographic studies of carbohydrates
    • Jeffrey G.A. Crystallographic studies of carbohydrates. Acta Crystallogr. B. 46 (1990) 89-103
    • (1990) Acta Crystallogr. B. , vol.46 , pp. 89-103
    • Jeffrey, G.A.1
  • 17
    • 0027430967 scopus 로고
    • A new biochemical marker for joint injury. Analysis of YKL-40 in serum and synovial fluid
    • Johansen J.S., Jensen H.S., and Price P.A. A new biochemical marker for joint injury. Analysis of YKL-40 in serum and synovial fluid. Br. J. Rheumatol. 32 (1993) 949-955
    • (1993) Br. J. Rheumatol. , vol.32 , pp. 949-955
    • Johansen, J.S.1    Jensen, H.S.2    Price, P.A.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard W.J.M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47 (1991) 110-119
    • (1991) Acta Crystallogr. A. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, W.J.M.4
  • 21
    • 0028063457 scopus 로고
    • neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2initiated tumors
    • Morrison B.W., and Leder P. neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2initiated tumors. Oncogene 9 (1994) 3417-3426
    • (1994) Oncogene , vol.9 , pp. 3417-3426
    • Morrison, B.W.1    Leder, P.2
  • 22
    • 84920325457 scopus 로고
    • AMoRe: an automated package for moleucular replacement
    • Navaza J. AMoRe: an automated package for moleucular replacement. Acta Crystallogr. A. 50 (1994) 157-163
    • (1994) Acta Crystallogr. A. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 23
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics
    • Nieba L., Krebber A., and Pluckthun A. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal. Biochem. 234 (1996) 155-165
    • (1996) Anal. Biochem. , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collection in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
  • 26
    • 0023835707 scopus 로고
    • Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period Biochem
    • Rejman J.J., and Hurley W.L. Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period Biochem. Biophys. Res. Commun. 150 (1988) 329-334
    • (1988) Biophys. Res. Commun. , vol.150 , pp. 329-334
    • Rejman, J.J.1    Hurley, W.L.2
  • 27
    • 0028911536 scopus 로고
    • Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins
    • Renkema G.H., Boot R.G., Muijsers A.O., Donker-Koopman W.E., and Aerts J.M.F.G. Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J. Biol. Chem. 270 (1995) 2198-2202
    • (1995) J. Biol. Chem. , vol.270 , pp. 2198-2202
    • Renkema, G.H.1    Boot, R.G.2    Muijsers, A.O.3    Donker-Koopman, W.E.4    Aerts, J.M.F.G.5
  • 28
    • 0029039184 scopus 로고
    • Identification of a 38 kDa heparin-binding glycoprotein (gp38k) in differentiating vascular smooth muscle cells as a member of a group of proteins associated with tissue remodeling
    • Shackelton L.M., Mann D.M., and Millis A.J. Identification of a 38 kDa heparin-binding glycoprotein (gp38k) in differentiating vascular smooth muscle cells as a member of a group of proteins associated with tissue remodeling. J. Biol. Chem. 270 (1995) 13076-13083
    • (1995) J. Biol. Chem. , vol.270 , pp. 13076-13083
    • Shackelton, L.M.1    Mann, D.M.2    Millis, A.J.3
  • 30
    • 0026773069 scopus 로고
    • Apoptotic cell death and tissue remodelling during mouse mammary gland involution
    • Strange R., Li F., Saurer S., Burkhardt A., and Friis R.R. Apoptotic cell death and tissue remodelling during mouse mammary gland involution. Development 115 (1992) 49-58
    • (1992) Development , vol.115 , pp. 49-58
    • Strange, R.1    Li, F.2    Saurer, S.3    Burkhardt, A.4    Friis, R.R.5
  • 31
    • 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., Chang A.C., 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    Chang, A.C.4    Chou, C.C.5    Hsiao, C.D.6
  • 32
    • 0028822007 scopus 로고
    • Surface plasmon resonance and its use in biomolecular interaction analysis (BIA)
    • Szabo A., Stolz L., and Granzow R. Surface plasmon resonance and its use in biomolecular interaction analysis (BIA). Curr. Opin. Struct. Biol. 5 (1995) 699-705
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 699-705
    • Szabo, A.1    Stolz, L.2    Granzow, R.3
  • 33
    • 0022004788 scopus 로고
    • Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies
    • Tabary F., and Frenoy J.P. Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies. Biochem. J. 229 (1985) 687-692
    • (1985) Biochem. J. , vol.229 , pp. 687-692
    • Tabary, F.1    Frenoy, J.P.2
  • 34
    • 7444250123 scopus 로고    scopus 로고
    • The crystal structure of Ym1 at 1.31 Å resolution
    • Tsai M.L., Liaw S.H., and Chang N.C. The crystal structure of Ym1 at 1.31 Å resolution. J. Struct. Biol. 148 (2004) 290-296
    • (2004) J. Struct. Biol. , vol.148 , pp. 290-296
    • Tsai, M.L.1    Liaw, S.H.2    Chang, N.C.3


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