메뉴 건너뛰기




Volumn 390, Issue 3, 2009, Pages 457-466

Structural Characterization of a Lectin from the Mushroom Marasmius oreades in Complex with the Blood Group B Trisaccharide and Calcium

Author keywords

blood group recognition; carbohydrate recognition; fungal agglutinin; protein carbohydrate interaction; X ray crystal structure

Indexed keywords

CALCIUM ION; HOMODIMER; LECTIN; TRISACCHARIDE;

EID: 67449099042     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.074     Document Type: Article
Times cited : (33)

References (31)
  • 1
    • 0010102516 scopus 로고
    • Phytagglutinins present in Marasmius oreades
    • Elo J., and Estola E. Phytagglutinins present in Marasmius oreades. Ann. Med. Exp. Biol. Fenn. 30 (1952) 165-167
    • (1952) Ann. Med. Exp. Biol. Fenn. , vol.30 , pp. 165-167
    • Elo, J.1    Estola, E.2
  • 3
    • 0037177879 scopus 로고    scopus 로고
    • The mushroom Marasmius oreades lectin is a blood group type B agglutinin that recognizes the Galα1,3Gal and Galα1,3Galβ1,4GlcNAc porcine xenotransplantation epitopes with high affinity
    • Winter H.C., Mostafapour K., and Goldstein I.J. The mushroom Marasmius oreades lectin is a blood group type B agglutinin that recognizes the Galα1,3Gal and Galα1,3Galβ1,4GlcNAc porcine xenotransplantation epitopes with high affinity. J. Biol. Chem. 277 (2002) 14996-15001
    • (2002) J. Biol. Chem. , vol.277 , pp. 14996-15001
    • Winter, H.C.1    Mostafapour, K.2    Goldstein, I.J.3
  • 4
    • 0037177865 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the Galα1,3Gal high affinity lectin from the mushroom Marasmius oreades
    • Kruger R.P., Winter H.C., Simonson-Leff N., Stuckey J.A., Goldstein I.J., and Dixon J.E. Cloning, expression, and characterization of the Galα1,3Gal high affinity lectin from the mushroom Marasmius oreades. J. Biol. Chem. 277 (2002) 15002-15005
    • (2002) J. Biol. Chem. , vol.277 , pp. 15002-15005
    • Kruger, R.P.1    Winter, H.C.2    Simonson-Leff, N.3    Stuckey, J.A.4    Goldstein, I.J.5    Dixon, J.E.6
  • 5
    • 0037485923 scopus 로고    scopus 로고
    • Characterization of the recognition of blood group B trisaccharide derivatives by the lectin from Marasmius oreades using frontal affinity chromatography-mass spectrometry
    • Rempel B.P., Winter H.C., Goldstein I.J., and Hindsgaul O. Characterization of the recognition of blood group B trisaccharide derivatives by the lectin from Marasmius oreades using frontal affinity chromatography-mass spectrometry. Glycoconjugate J. 19 (2003) 175-180
    • (2003) Glycoconjugate J. , vol.19 , pp. 175-180
    • Rempel, B.P.1    Winter, H.C.2    Goldstein, I.J.3    Hindsgaul, O.4
  • 6
    • 0038657839 scopus 로고    scopus 로고
    • Studies on Galα3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin
    • Teneberg S., Alsén B., Ångström J., Winter H.C., and Goldstein I.J. Studies on Galα3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin. Glycobiology 13 (2003) 479-486
    • (2003) Glycobiology , vol.13 , pp. 479-486
    • Teneberg, S.1    Alsén, B.2    Ångström, J.3    Winter, H.C.4    Goldstein, I.J.5
  • 7
    • 0017413222 scopus 로고
    • Five α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds
    • Murphy L.A., and Goldstein I.J. Five α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds. J. Biol. Chem. 252 (1977) 4739-4742
    • (1977) J. Biol. Chem. , vol.252 , pp. 4739-4742
    • Murphy, L.A.1    Goldstein, I.J.2
  • 8
    • 0017510167 scopus 로고
    • Ptilota plumosa, a new source of a blood-group B specific lectin
    • Rogers D.J., Blunden G., and Evans P.R. Ptilota plumosa, a new source of a blood-group B specific lectin. Med. Lab. Sci. 34 (1977) 193-200
    • (1977) Med. Lab. Sci. , vol.34 , pp. 193-200
    • Rogers, D.J.1    Blunden, G.2    Evans, P.R.3
  • 9
    • 0022432903 scopus 로고
    • Blood group B-specific lectin of Plecoglossus altivelis (Ayu fish) eggs
    • Sakakibara F., Kawauchi H., and Takayanagi G. Blood group B-specific lectin of Plecoglossus altivelis (Ayu fish) eggs. Biochim. Bophys. Acta 26 (1985) 103-111
    • (1985) Biochim. Bophys. Acta , vol.26 , pp. 103-111
    • Sakakibara, F.1    Kawauchi, H.2    Takayanagi, G.3
  • 10
    • 0037155263 scopus 로고    scopus 로고
    • 4. X-ray crystal structure of the complex and molecular dynamics characterization of the binding site
    • 4. X-ray crystal structure of the complex and molecular dynamics characterization of the binding site. J. Biol. Chem. 277 (2002) 6615-6621
    • (2002) J. Biol. Chem. , vol.277 , pp. 6615-6621
    • Tempel, W.1    Tschampel, S.2    Woods, R.J.3
  • 12
    • 34248153179 scopus 로고    scopus 로고
    • Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope
    • Grahn E., Askarieh G., Holmner Å., Tateno H., Winter H.C., Goldstein I.J., and Krengel U. Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope. J. Mol. Biol. 369 (2007) 710-721
    • (2007) J. Mol. Biol. , vol.369 , pp. 710-721
    • Grahn, E.1    Askarieh, G.2    Holmner, Å.3    Tateno, H.4    Winter, H.C.5    Goldstein, I.J.6    Krengel, U.7
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., and Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. Sect. A 47 (1991) 392-400
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 14
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • Kleywegt G.J., and Jones T.A. Phi/Psi-chology: Ramachandran revisited. Structure 4 (1996) 1395-1400
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 16
    • 34249822248 scopus 로고    scopus 로고
    • Structural basis for the recognition of blood group trisaccharides by norovirus
    • Cao S., Lou Z., Tan M., Chen Y., Liu Y., Zhang Z., et al. Structural basis for the recognition of blood group trisaccharides by norovirus. J. Virol. 81 (2007) 5949-5957
    • (2007) J. Virol. , vol.81 , pp. 5949-5957
    • Cao, S.1    Lou, Z.2    Tan, M.3    Chen, Y.4    Liu, Y.5    Zhang, Z.6
  • 17
    • 45549100630 scopus 로고    scopus 로고
    • Divergent modes of glycan recognition by a new family of carbohydrate-binding modules
    • Gregg K.J., Finn R., Abbot D.W., and Boraston A.B. Divergent modes of glycan recognition by a new family of carbohydrate-binding modules. J. Biol. Chem. 283 (2008) 12604-12613
    • (2008) J. Biol. Chem. , vol.283 , pp. 12604-12613
    • Gregg, K.J.1    Finn, R.2    Abbot, D.W.3    Boraston, A.B.4
  • 18
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins
    • Harding M.M. The geometry of metal-ligand interactions relevant to proteins. Acta Crystallogr. Sect. D 55 (1999) 1432-1443
    • (1999) Acta Crystallogr. Sect. D , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 19
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding M.M. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. Sect. D 57 (2001) 401-411
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 21
    • 0000596916 scopus 로고
    • Towards an understanding of the effects of calcium on protein structure and function
    • Strynadka N.C.J., and James M.N.G. Towards an understanding of the effects of calcium on protein structure and function. Curr. Opin. Struct. Biol. 1 (1991) 905-914
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 905-914
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 22
  • 23
    • 4544362981 scopus 로고    scopus 로고
    • Cloning, expression in Escherichia coli and characterization of the recombinant Neu5Acα2,6Galβ1,4GlcNAc-specific high-affinity lectin and its mutants from the mushroom Polyporus squamosus
    • Tateno H., Winter H.C., and Goldstein I.J. Cloning, expression in Escherichia coli and characterization of the recombinant Neu5Acα2,6Galβ1,4GlcNAc-specific high-affinity lectin and its mutants from the mushroom Polyporus squamosus. Biochem. J. 382 (2004) 667-675
    • (2004) Biochem. J. , vol.382 , pp. 667-675
    • Tateno, H.1    Winter, H.C.2    Goldstein, I.J.3
  • 24
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. 26 (1992)
    • (1992) Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. , vol.26
    • Leslie, A.G.W.1
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 27
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 28
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 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 M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.