메뉴 건너뛰기




Volumn 332, Issue 1, 2003, Pages 217-228

Structural basis of the carbohydrate specificities of jacalin: An X-ray and modeling study

Author keywords

Carbohydrate specificity; Glycoproteins; Moraceae lectin; O C H interactions; Water bridges

Indexed keywords

CARBOHYDRATE DERIVATIVE; DISACCHARIDE; GALACTOSE; JACALIN; WATER;

EID: 0042511948     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00901-X     Document Type: Article
Times cited : (60)

References (45)
  • 1
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • Sharon N., Lis H. Lectins as cell recognition molecules. Science. 246:1989;227-246.
    • (1989) Science , vol.246 , pp. 227-246
    • Sharon, N.1    Lis, H.2
  • 2
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: Carbohydrate specific proteins that mediate cellular recognition
    • Lis H., Sharon N. Lectins: carbohydrate specific proteins that mediate cellular recognition. Chem. Rev. 98:1998;637-674.
    • (1998) Chem. Rev. , vol.98 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 4
    • 0032871411 scopus 로고    scopus 로고
    • New animal lectin structures
    • Rini J. New animal lectin structures. Curr. Opin. Struct. Biol. 9:1999;578-584.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 578-584
    • Rini, J.1
  • 7
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: Occurrence, biochemistry, functions and applications
    • Rudiger H., Gabius H.J. Plant lectins: occurrence, biochemistry, functions and applications. Glycoconj. J. 18:2001;589-613.
    • (2001) Glycoconj. J. , vol.18 , pp. 589-613
    • Rudiger, H.1    Gabius, H.J.2
  • 8
    • 0034851060 scopus 로고    scopus 로고
    • Mannose-binding plant lectins: Different structural scaffolds for a common sugar-recognition process
    • Barre A., Bourner Y., Van Damme E.J., Peumans W.J., Rouge P. Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process. Biochimie. 83:2001;645-651.
    • (2001) Biochimie , vol.83 , pp. 645-651
    • Barre, A.1    Bourner, Y.2    Van Damme, E.J.3    Peumans, W.J.4    Rouge, P.5
  • 10
    • 0036295206 scopus 로고    scopus 로고
    • Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-D-mannose: Implications to the generation of carbohydrate specificity
    • Pratap J.V., Jeyaprakash A.A., Rani P.G., Sekar K., Surolia A., Vijayan M. Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-D-mannose: implications to the generation of carbohydrate specificity. J. Mol. Biol. 317:2002;237-247.
    • (2002) J. Mol. Biol. , vol.317 , pp. 237-247
    • Pratap, J.V.1    Jeyaprakash, A.A.2    Rani, P.G.3    Sekar, K.4    Surolia, A.5    Vijayan, M.6
  • 11
    • 0037093547 scopus 로고    scopus 로고
    • Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose
    • Bourne Y., Astoul C.H., Zamboni V., Peumans W.J., Menu-Bouaouiche L., van Damme E.J.M., et al. Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose. Biochem. J. 364:2002;173-180.
    • (2002) Biochem. J. , vol.364 , pp. 173-180
    • Bourne, Y.1    Astoul, C.H.2    Zamboni, V.3    Peumans, W.J.4    Menu-Bouaouiche, L.5    Van Damme, E.J.M.6
  • 12
    • 0023212663 scopus 로고
    • Characterization of jacalin, the human IgA and IgD binding lectin from jackfruit
    • Aucouturier P., Mihaesco E., Mihaesco C., Preud'homme J.L. Characterization of jacalin, the human IgA and IgD binding lectin from jackfruit. Mol. Immunol. 24:1987;503-511.
    • (1987) Mol. Immunol. , vol.24 , pp. 503-511
    • Aucouturier, P.1    Mihaesco, E.2    Mihaesco, C.3    Preud'homme, J.L.4
  • 13
    • 0026559917 scopus 로고
    • Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [Artocarpus integrifolia (jackfruit) agglutinin]. Evidence for the presence of an internal repeat
    • Mahanta S.K., Sanker S., Rao N.V.S.A.V.P., Swamy M.J., Surolia A. Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [Artocarpus integrifolia (jackfruit) agglutinin]. Evidence for the presence of an internal repeat. Biochem. J. 284:1992;95-101.
    • (1992) Biochem. J. , vol.284 , pp. 95-101
    • Mahanta, S.K.1    Sanker, S.2    Rao, N.V.S.A.V.3    Swamy, M.J.4    Surolia, A.5
  • 14
    • 0027530010 scopus 로고
    • Isolation and characterization of cDNA clones encoding jacalin isolectins
    • Yang H., Czapla T.H. Isolation and characterization of cDNA clones encoding jacalin isolectins. J. Biol. Chem. 268:1993;5905-5910.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5905-5910
    • Yang, H.1    Czapla, T.H.2
  • 15
    • 0032520680 scopus 로고    scopus 로고
    • Jacalin: A jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research
    • Kabir S. Jacalin: a jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research. J. Immunol. Methods. 212:1998;193-211.
    • (1998) J. Immunol. Methods , vol.212 , pp. 193-211
    • Kabir, S.1
  • 16
    • 0019472790 scopus 로고
    • Lectin(s) extracted from seeds of Artocarpus integrifolia (jackfruit): Potent and selective stimulator(s) of distinct human T and B cell functions
    • Bunn-Moreno M.M., Campos-Neto A. Lectin(s) extracted from seeds of Artocarpus integrifolia (jackfruit): potent and selective stimulator(s) of distinct human T and B cell functions. J. Immunol. 127:1981;427.
    • (1981) J. Immunol. , vol.127 , pp. 427
    • Bunn-Moreno, M.M.1    Campos-Neto, A.2
  • 19
    • 0028359082 scopus 로고
    • Jacalin, a lectin with anti-HIV properties, and HIV-I gp120 envelope protein interact with distinct regions of the CD4 molecule
    • Corbeau P., Haran M., Binz H., Devanux C. Jacalin, a lectin with anti-HIV properties, and HIV-I gp120 envelope protein interact with distinct regions of the CD4 molecule. Mol. Immunol. 31:1994;569-575.
    • (1994) Mol. Immunol. , vol.31 , pp. 569-575
    • Corbeau, P.1    Haran, M.2    Binz, H.3    Devanux, C.4
  • 20
    • 0029123329 scopus 로고
    • + cells against HIV-I, binds to the external envelope glycoprotein gp120
    • + cells against HIV-I, binds to the external envelope glycoprotein gp120. Immunol. Letters. 47:1995;141-143.
    • (1995) Immunol. Letters , vol.47 , pp. 141-143
    • Corbeau, P.1    Pasquali, J.L.2    Devaux, C.3
  • 21
    • 0027483787 scopus 로고
    • Perturbation of in vitro HIV pathogenic effects by peptides showing sequence similarities with the C2 conserved domain of gp120
    • Lafont V., Nicolas M., Dornand J., Liautard J.P., Favero J. Perturbation of in vitro HIV pathogenic effects by peptides showing sequence similarities with the C2 conserved domain of gp120. Immunol. Letters. 37:1993;249-250.
    • (1993) Immunol. Letters , vol.37 , pp. 249-250
    • Lafont, V.1    Nicolas, M.2    Dornand, J.3    Liautard, J.P.4    Favero, J.5
  • 22
    • 0027949101 scopus 로고
    • Jacalin, a lectin that inhibits in vitro HIV-1 infection, induces intracellular calcium increase via CD4 in cells lacking the CD3/TcR complex
    • Lafont V., Dornand J., d'Angeac A.D., Monier S., Alcover A., Favero J. Jacalin, a lectin that inhibits in vitro HIV-1 infection, induces intracellular calcium increase via CD4 in cells lacking the CD3/TcR complex. J. Leukoc. Biol. 56:1994;521-524.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 521-524
    • Lafont, V.1    Dornand, J.2    D'Angeac, A.D.3    Monier, S.4    Alcover, A.5    Favero, J.6
  • 23
    • 0029970952 scopus 로고    scopus 로고
    • The lectin jacalin triggers CD4-mediated lymphocyte signaling by binding CD4 through a protein-protein interaction
    • Lafont V., Dornand J., Covassin L., Liautard J.P., Favero J. The lectin jacalin triggers CD4-mediated lymphocyte signaling by binding CD4 through a protein-protein interaction. J. Leukoc. Biol. 59:1996;691-696.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 691-696
    • Lafont, V.1    Dornand, J.2    Covassin, L.3    Liautard, J.P.4    Favero, J.5
  • 24
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal(1-3)D-GalNAc)
    • Sastry M.V., Banarjee P., Patanjali S.R., Swamy M.J., Swarnalatha G.V., Surolia A. Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal(1-3)D-GalNAc). J. Biol. Chem. 261:1986;11726-11733.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 25
    • 0025141799 scopus 로고
    • Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study
    • Mahanta S.K., Sastry M.V., Surolia A. Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study. Biochem. J. 265:1990;831-840.
    • (1990) Biochem. J. , vol.265 , pp. 831-840
    • Mahanta, S.K.1    Sastry, M.V.2    Surolia, A.3
  • 26
    • 0036971194 scopus 로고    scopus 로고
    • Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes
    • Jeyaprakash A.A., Rani P.G., Reddy G.B., Banumathi S., Betzel C., Sekar K., et al. Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes. J. Mol. Biol. 321:2002;637-645.
    • (2002) J. Mol. Biol. , vol.321 , pp. 637-645
    • Jeyaprakash, A.A.1    Rani, P.G.2    Reddy, G.B.3    Banumathi, S.4    Betzel, C.5    Sekar, K.6
  • 27
    • 0035910278 scopus 로고    scopus 로고
    • Hydrogen bonds with π-acceptors in proteins: Frequencies and role in stabilizing local 3D structures
    • Steiner T., Koellner G. Hydrogen bonds with π-acceptors in proteins: frequencies and role in stabilizing local 3D structures. J. Mol. Biol. 305:2001;535-557.
    • (2001) J. Mol. Biol. , vol.305 , pp. 535-557
    • Steiner, T.1    Koellner, G.2
  • 29
    • 0037418604 scopus 로고    scopus 로고
    • Binding profile of Artocarpus integrifolia agglutinin (jacalin)
    • Wu M., Wu J.H., Lin L., Liu J. Binding profile of Artocarpus integrifolia agglutinin (jacalin). Life Sci. 72:2003;2285-2302.
    • (2003) Life Sci. , vol.72 , pp. 2285-2302
    • Wu, M.1    Wu, J.H.2    Lin, L.3    Liu, J.4
  • 30
    • 0032973358 scopus 로고    scopus 로고
    • Structural features of IgA molecules which contribute to IgA nephropathy
    • Allen A.C. Structural features of IgA molecules which contribute to IgA nephropathy. J. Nephrol. 12:1999;59-65.
    • (1999) J. Nephrol. , vol.12 , pp. 59-65
    • Allen, A.C.1
  • 31
    • 0033017675 scopus 로고    scopus 로고
    • Methodological approaches to the analysis of IgA1 O-glycosylation in IgA nephropathy
    • Allen A.C. Methodological approaches to the analysis of IgA1 O-glycosylation in IgA nephropathy. J. Nephrol. 12:1999;76-84.
    • (1999) J. Nephrol. , vol.12 , pp. 76-84
    • Allen, A.C.1
  • 32
    • 0036846005 scopus 로고    scopus 로고
    • The size, shape and specificity of the sugar-binding site of jacalin-related lectins is profoundly affected by the proteolytic cleavage of the subunits
    • Astoul C.H., Peumans W.J., van Damme E.J.M., Barre A., Bourne Y., Rouge P. The size, shape and specificity of the sugar-binding site of jacalin-related lectins is profoundly affected by the proteolytic cleavage of the subunits. Biochem. J. 367:2002;817-824.
    • (2002) Biochem. J. , vol.367 , pp. 817-824
    • Astoul, C.H.1    Peumans, W.J.2    Van Damme, E.J.M.3    Barre, A.4    Bourne, Y.5    Rouge, P.6
  • 33
    • 0026489530 scopus 로고
    • Poly-N-acetyllactosaminyl O-glycans attached to leukosialin
    • Maemura K., Fukuda M. Poly-N-acetyllactosaminyl O-glycans attached to leukosialin. J. Biol. Chem. 267:1992;24379-24386.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24379-24386
    • Maemura, K.1    Fukuda, M.2
  • 34
    • 0032937844 scopus 로고    scopus 로고
    • A statistical analysis of N- and O-glycan linkage conformations from crystallographic data
    • Petrescu A.J., Petrescu S.M., Dwek R.A., Wormald M.R. A statistical analysis of N- and O-glycan linkage conformations from crystallographic data. Glycobiology. 9:1999;343-352.
    • (1999) Glycobiology , vol.9 , pp. 343-352
    • Petrescu, A.J.1    Petrescu, S.M.2    Dwek, R.A.3    Wormald, M.R.4
  • 35
    • 0020263478 scopus 로고
    • α-D-galactose-specific lectin from jackfruit (Artocarpus integrifolia) seed
    • Kumar S.G., Appukuttan P.S., Basu D. α-D-galactose-specific lectin from jackfruit (Artocarpus integrifolia) seed. J. Biosci. 4:1993;257-261.
    • (1993) J. Biosci. , vol.4 , pp. 257-261
    • Kumar, S.G.1    Appukuttan, P.S.2    Basu, D.3
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, Sweet R.M. New York: Academic Press
    • Otwinowsky Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter C.W. Jr, Sweet R.M. Macromolecular Crystallography, Part A, Methods of Enzymology. vol. 276:1997;307-326 Academic Press, New York.
    • (1997) Macromolecular Crystallography, Part A, Methods of Enzymology , vol.276 , pp. 307-326
    • Otwinowsky, Z.1    Minor, W.2
  • 38
    • 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
  • 39
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;445-449.
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 445-449
    • Navaza, J.1
  • 40
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • Brunger A.T., Adams P.D., Rice L.M. Recent developments for the efficient crystallographic refinement of macromolecular structures. Curr. Opin. Struct. Biol. 8:1998;606-611.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 606-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 41
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T.A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11:1978;268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 42
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1993;1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 43
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen G.E. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallog. 30:1997;1160-1161.
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 44
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:1994;777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 45
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.