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Volumn 117, Issue 1, 1996, Pages 16-23

A triclinic crystal form of the lectin concanavalin A

Author keywords

[No Author keywords available]

Indexed keywords

CONCANAVALIN A;

EID: 0030198976     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1996.0065     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0015351812 scopus 로고
    • Activation of B lymphocytes by locally concentrated concanavalin A
    • Andersson, J., Edelman, G. M., Moller, G., and Sjoberg, O. (1972) Activation of B lymphocytes by locally concentrated concanavalin A, Eur. J. Immunol. 2, 233-235.
    • (1972) Eur. J. Immunol. , vol.2 , pp. 233-235
    • Andersson, J.1    Edelman, G.M.2    Moller, G.3    Sjoberg, O.4
  • 2
    • 0017262126 scopus 로고
    • New evidence on the location of the saccharide-binding site of concanavalin A
    • Becker, J. W., Reeke, G. N., Jr., Cunningham, B. A., and Edelman, G. M. (1976) New evidence on the location of the saccharide-binding site of concanavalin A, Nature (London) 259, 406-409.
    • (1976) Nature (London) , vol.259 , pp. 406-409
    • Becker, J.W.1    Reeke G.N., Jr.2    Cunningham, B.A.3    Edelman, G.M.4
  • 5
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. (1992b) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures, Nature 335, 472-475.
    • (1992) Nature , vol.335 , pp. 472-475
    • Brunger, A.T.1
  • 10
    • 0015516458 scopus 로고
    • Structure of concanavalin A at 2.4-Å resolution
    • Hardman, K. D., and Ainsworth, C. F. (1972) Structure of concanavalin A at 2.4-Å resolution, Biochemistry, 11, 4910-4919.
    • (1972) Biochemistry , vol.11 , pp. 4910-4919
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 11
    • 0019917071 scopus 로고
    • Manganese and calcium binding sites of concanavalin A
    • Hardman, K. D., Agarwal, R. C., and Freiser, M. J. (1982) Manganese and calcium binding sites of concanavalin A, J. Mol. Biol. 157, 69-86.
    • (1982) J. Mol. Biol. , vol.157 , pp. 69-86
    • Hardman, K.D.1    Agarwal, R.C.2    Freiser, M.J.3
  • 12
    • 0014552290 scopus 로고
    • The interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells
    • Imhar, M., and Sachs, L. (1969) The interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells, Proc. Nat. Acad. Sci. USA 63, 1418-1425.
    • (1969) Proc. Nat. Acad. Sci. USA , vol.63 , pp. 1418-1425
    • Imhar, M.1    Sachs, L.2
  • 13
    • 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. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector, J. Appl. Crystallogr. 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 15
    • 0014425864 scopus 로고
    • The molecular weight of concanavalin A
    • Kalb, A. J., and Lustig, A. (1968) The molecular weight of concanavalin A, Biochim. Biophys. Acta 168, 366-367.
    • (1968) Biochim. Biophys. Acta , vol.168 , pp. 366-367
    • Kalb, A.J.1    Lustig, A.2
  • 16
    • 0014346580 scopus 로고
    • Metal-binding sites of concanavalin A and their role in the binding of α-methyl-D-glucopyranoside
    • Kalb, A. J., and Levitzki, A. (1968) Metal-binding sites of concanavalin A and their role in the binding of α-methyl-D-glucopyranoside, Biochem. J. 109, 669-672.
    • (1968) Biochem. J. , vol.109 , pp. 669-672
    • Kalb, A.J.1    Levitzki, A.2
  • 18
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D., 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.3    Thornton, J.M.4
  • 20
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzatti, V. (1952) Traitement statistique des erreurs dans la determination des structures cristallines, Acta Crystallogr. 5, 802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzatti, V.1
  • 21
    • 0015508072 scopus 로고
    • The molecular weight and stability of concanavalin A
    • McKenzie, G. H., Sawyer, W. H., and Nichol, L. W. (1972) The molecular weight and stability of concanavalin A, Biochim. Biophys. Acta 263, 283-293.
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 283-293
    • McKenzie, G.H.1    Sawyer, W.H.2    Nichol, L.W.3
  • 23
    • 0028038824 scopus 로고
    • Refined structure of concanavalin A complexed with methyl-a-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure
    • Naismith, J. H., Emmerich, C., Habash, J., Harrop, S. J., Helliwell, J. R., Hunter, W. N., Raftery, J., Kalb(Gilboa), A. J., and Yariv, J. (1994) Refined structure of concanavalin A complexed with methyl-a-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure, Acta Crystallogr. D50, 847-858.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 847-858
    • Naismith, J.H.1    Emmerich, C.2    Habash, J.3    Harrop, S.J.4    Helliwell, J.R.5    Hunter, W.N.6    Raftery, J.7    Kalb, A.J.8    Yariv, J.9
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: An automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0004124018 scopus 로고
    • Chapman & Hall, London
    • Sharon, N., and Lis, H. (1989a) Lectins, Chapman & Hall, London.
    • (1989) Lectins
    • Sharon, N.1    Lis, H.2
  • 27
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • Sharon, N., and Lis, H. (1989b) Lectins as cell recognition molecules, Science 246, 227-234.
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 28
    • 0025222989 scopus 로고
    • Legume lectins - A large family of homologous proteins
    • Sharon, N., and Lis, H. (1990) Legume lectins - A large family of homologous proteins, FASEB J. 4, 3198-3208.
    • (1990) FASEB J. , vol.4 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 29
    • 0018419328 scopus 로고
    • Crystal structure of demetallized concanavalin A: The metal-binding region
    • Shoham, M., Yonath, A., Sussman, J. L., Moult, J., Traub, W., and Kalb, A. J. (1979) Crystal structure of demetallized concanavalin A: The metal-binding region, J. Mol. Biol. 131, 137-155.
    • (1979) J. Mol. Biol. , vol.131 , pp. 137-155
    • Shoham, M.1    Yonath, A.2    Sussman, J.L.3    Moult, J.4    Traub, W.5    Kalb, A.J.6
  • 30
    • 0000923505 scopus 로고
    • The identification of the haemagglutinin of jack bean with concanavalin A
    • Sumner, J. B., and Howell, S. F. (1936) The identification of the haemagglutinin of Jack bean with concanavalin A, J. Bacteriol. 32, 227-237.
    • (1936) J. Bacteriol. , vol.32 , pp. 227-237
    • Sumner, J.B.1    Howell, S.F.2
  • 31
    • 0000506911 scopus 로고
    • High-resolution crystallographic studies of native concanavalin A using rapid Laue data collection methods and the introduction of a monochromatic large-angle oscillation technique (LOT)
    • Weisgerber, S., and Helliwell, J. R. (1993) High-resolution crystallographic studies of native concanavalin A using rapid Laue data collection methods and the introduction of a monochromatic large-angle oscillation technique (LOT), J. Chem. Soc. Faraday Trans. 89, 2667-2675.
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2667-2675
    • Weisgerber, S.1    Helliwell, J.R.2
  • 32
    • 0000952666 scopus 로고
    • Structure and funtion of leguminosae lectins
    • Franz, H. (Ed.), Springer-Verlag, Berlin
    • Van Driessche, E. (1988) Structure and funtion of leguminosae lectins, in Franz, H. (Ed.), Advances in Lectin Research, Vol. 1, pp. 73-134, Springer-Verlag, Berlin.
    • (1988) Advances in Lectin Research , vol.1 , pp. 73-134
    • Van Driessche, E.1
  • 33
    • 0015307992 scopus 로고
    • Restriction of the mobility of lymphocyte immunoglobulin receptors by concanavalin A
    • Yahara, I., and Edelman, G. M. (1972) Restriction of the mobility of lymphocyte immunoglobulin receptors by concanavalin A, Proc. Nat. Acad. Sci. USA 69, 608-612.
    • (1972) Proc. Nat. Acad. Sci. USA , vol.69 , pp. 608-612
    • Yahara, I.1    Edelman, G.M.2
  • 34
    • 0015791613 scopus 로고
    • The effects of concanavalin A on the mobility of lymphocyte surface receptors
    • Yahara, I., and Edelman, G. M. (1973) The effects of concanavalin A on the mobility of lymphocyte surface receptors, Exp. Cell Res. 81, 143-155.
    • (1973) Exp. Cell Res. , vol.81 , pp. 143-155
    • Yahara, I.1    Edelman, G.M.2
  • 35
    • 0014402071 scopus 로고
    • The interaction of concanavalin A with methyl-α-D-glucopyranoside
    • Yariv, J., Kalb, A. J., and Levitzki, A. (1968) The interaction of concanavalin A with methyl-α-D-glucopyranoside, Biochim. Biophys. Acta 165, 303-305.
    • (1968) Biochim. Biophys. Acta , vol.165 , pp. 303-305
    • Yariv, J.1    Kalb, A.J.2    Levitzki, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.