메뉴 건너뛰기




Volumn 26, Issue 1, 1996, Pages 55-65

Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment

Author keywords

anti protein Fab; antibody antigen complex; avian lysozyme

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; LYSOZYME;

EID: 10144235477     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F     Document Type: Article
Times cited : (27)

References (57)
  • 1
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution
    • Amit, A.G., Mariuzza, R.A., Phillips, S.E.V., Poljak, R.J. Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233:747-753, 1986.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.V.3    Poljak, R.J.4
  • 4
    • 0002834361 scopus 로고
    • Neuraminidase: Enzyme and antigen
    • Krug, R.M. (ed.). New York: Plenum
    • Colman, P.M. Neuraminidase: enzyme and antigen. In: *The Influenza Viruses.* Krug, R.M. (ed.). New York: Plenum, 1989: 175-218.
    • (1989) The Influenza Viruses , pp. 175-218
    • Colman, P.M.1
  • 5
    • 0025151612 scopus 로고
    • Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding
    • Bhat, T.N. Bentley, G.A., Fischmann, T.O., Boulot, G., Poljak, R.J. Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature 347:483-485, 1990.
    • (1990) Nature , vol.347 , pp. 483-485
    • Bhat, T.N.1    Bentley, G.A.2    Fischmann, T.O.3    Boulot, G.4    Poljak, R.J.5
  • 6
    • 0025059666 scopus 로고
    • Three-dimensional structure of an idiotope-anti-idiotope complex
    • Bentley, G.A., Boulot, G., Riottot, M.M., Poljak, R.J. Three-dimensional structure of an idiotope-anti-idiotope complex. Nature 348:254-257, 1990.
    • (1990) Nature , vol.348 , pp. 254-257
    • Bentley, G.A.1    Boulot, G.2    Riottot, M.M.3    Poljak, R.J.4
  • 8
    • 0026781840 scopus 로고
    • Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex
    • Tulip, W.R., Varghese, J.N., Laver, W.G., Webster, R.G., Colman, P.M. Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex. J. Mol. Biol. 227:122-148, 1992.
    • (1992) J. Mol. Biol. , vol.227 , pp. 122-148
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Webster, R.G.4    Colman, P.M.5
  • 9
    • 0026668006 scopus 로고
    • Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface
    • Tulip, W.R., Varghese, J.N., Webster, R.G., Laver, W.G., Colman, P.M. Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface. J. Mol. Biol. 227:149-159, 1992.
    • (1992) J. Mol. Biol. , vol.227 , pp. 149-159
    • Tulip, W.R.1    Varghese, J.N.2    Webster, R.G.3    Laver, W.G.4    Colman, P.M.5
  • 13
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody, D44.1
    • Braden, B.C., Souchon, H., Eiselé, J.-L., Bentley, G.A., Bhat, T.N., Navaza, J., Poljak, R.J. Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody, D44.1. J. Mol. Biol. 243:767-781, 1994.
    • (1994) J. Mol. Biol. , vol.243 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eiselé, J.-L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 14
    • 0028774037 scopus 로고
    • The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody
    • Malby, R.L., Tulip, W.R., Harley, V.R., McKimm-Breschkin, J.L., Laver, W.G., Webster, R.G., Colman, P.M. The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody. Structure 2:733-746, 1994.
    • (1994) Structure , vol.2 , pp. 733-746
    • Malby, R.L.1    Tulip, W.R.2    Harley, V.R.3    McKimm-Breschkin, J.L.4    Laver, W.G.5    Webster, R.G.6    Colman, P.M.7
  • 16
    • 0027956976 scopus 로고
    • Exploring the mimicry of polysaccharide antigens by antiidiotypic antibodies: The crystallization, molecular replacement, and refinement to 2.8 A resolution of an idiotope-anti-idiotipe Fab complex and of the unliganded anti-idiotope Fab
    • Evans, S.V., Rose, D.R., To, R., Young, N.M., Bundle, D.R. Exploring the mimicry of polysaccharide antigens by antiidiotypic antibodies: The crystallization, molecular replacement, and refinement to 2.8 A resolution of an idiotope-anti-idiotipe Fab complex and of the unliganded anti-idiotope Fab. J. Mol. Biol. 241:691-705, 1994.
    • (1994) J. Mol. Biol. , vol.241 , pp. 691-705
    • Evans, S.V.1    Rose, D.R.2    To, R.3    Young, N.M.4    Bundle, D.R.5
  • 17
    • 0028980629 scopus 로고
    • Structure of an antibody-lysozyme complex: Unexpected effect of a conservative mutation
    • Chacko, S., Silverton, E., Ram-Morgan, L., Smith-Gill, S., Cohen, G., Davies, D. Structure of an antibody-lysozyme complex: unexpected effect of a conservative mutation. J. Mol. Biol. 245:261-274, 1995.
    • (1995) J. Mol. Biol. , vol.245 , pp. 261-274
    • Chacko, S.1    Silverton, E.2    Ram-Morgan, L.3    Smith-Gill, S.4    Cohen, G.5    Davies, D.6
  • 19
    • 0028828994 scopus 로고
    • The crystal structure of the antibody N10 - Staphylococcal nuclease complex at 2.9 A resolution
    • Bossart-Whitaker, P., Chang, C., Novotny, J., Benjamin, D.C., Sheriff, S. The crystal structure of the antibody N10 - staphylococcal nuclease complex at 2.9 A resolution. J. Mol. Biol. 253:559-575, 1995.
    • (1995) J. Mol. Biol. , vol.253 , pp. 559-575
    • Bossart-Whitaker, P.1    Chang, C.2    Novotny, J.3    Benjamin, D.C.4    Sheriff, S.5
  • 21
    • 0030047926 scopus 로고    scopus 로고
    • The refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg white lysozyme
    • Cohen, G.H., Sheriff, S., Davies, D.R. The refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg white lysozyme. Acta Crystallogr. D 52:315-326, 1996.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 315-326
    • Cohen, G.H.1    Sheriff, S.2    Davies, D.R.3
  • 24
    • 0021123386 scopus 로고
    • Three dimensional structure of an antigenic mutant of the influenza virus haemmagglutinin
    • Knossow, M. Daniels, R.S., Douglas, A.R., Skehel, J.J., Wiley, D.C. Three dimensional structure of an antigenic mutant of the influenza virus haemmagglutinin. Nature 311:678-680, 1984.
    • (1984) Nature , vol.311 , pp. 678-680
    • Knossow, M.1    Daniels, R.S.2    Douglas, A.R.3    Skehel, J.J.4    Wiley, D.C.5
  • 25
    • 0001762604 scopus 로고
    • Some methods to examine the interaction between two molecules
    • Sheriff, S. Some methods to examine the interaction between two molecules. Immunomethods 3:222-227, 1993.
    • (1993) Immunomethods , vol.3 , pp. 222-227
    • Sheriff, S.1
  • 26
    • 0026575333 scopus 로고
    • Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme
    • Lavoie, T.B. Drohan, W.N., Smith-Gill, S.J. Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme. J. Immunol 148:503-513, 1992.
    • (1992) J. Immunol , vol.148 , pp. 503-513
    • Lavoie, T.B.1    Drohan, W.N.2    Smith-Gill, S.J.3
  • 29
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerchmidt, A., Pflugrath, J.W. Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Crystallogr. 20:306-315, 1987.
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 306-315
    • Messerchmidt, A.1    Pflugrath, J.W.2
  • 33
    • 84967852329 scopus 로고
    • MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald, P.M.D. MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Crystallogr. 21: 273-278, 1988.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 34
    • 85055704314 scopus 로고
    • Experiences with a new translation-function program
    • Fujinaga, M., Read, R.J. Experiences with a new translation-function program. J. Appl. Crystallogr. 20:517-521, 1987.
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 517-521
    • Fujinaga, M.1    Read, R.J.2
  • 36
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F., Matthews, B.W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A 43: 489-501, 1987.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 38
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. The free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-474, 1992.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 39
  • 40
    • 0014690368 scopus 로고
    • Immunological prediction of sequence differences among proteins: Chemical comparison of chicken, quail and pheasant lysozymes
    • Arnheim, N., Prager, E.M., Wilson, A.C. Immunological prediction of sequence differences among proteins: Chemical comparison of chicken, quail and pheasant lysozymes. J. Biol. Chem. 244:2085-2094, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2085-2094
    • Arnheim, N.1    Prager, E.M.2    Wilson, A.C.3
  • 41
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:795-798, 1993.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-798
    • Kabsch, W.1
  • 42
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein structure refinement
    • Engh, R.A., Huber, R. Accurate bond and angle parameters for x-ray protein structure refinement. Acta Crystallogr. A 47:392-400, 1991.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 44
    • 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., Kjeldgaard, M. "Improved Methods for Building Protein Models in Electron Density Maps and the Location of Errors in These Models", Acta Crystallogr. A 47:110-119, 1991.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M.L. Analytical molecular surface calculation. J. Appl. Crystallogr. 16:548-558, 1983.
    • (1983) J. Appl. Crystallogr. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 47
    • 0029140564 scopus 로고
    • The influence of temperature on lysozyme crystals
    • Kurinov, I.V., Harrison, R.W. The influence of temperature on lysozyme crystals. Acta Crystallogr. D 51:98-109, 1995.
    • (1995) Acta Crystallogr. D , vol.51 , pp. 98-109
    • Kurinov, I.V.1    Harrison, R.W.2
  • 48
    • 84912964993 scopus 로고
    • Refinement of triclinic lysozyme. II. The method of stereochemically restrained least squares
    • Ramanadham, M., Sieker, L.C., Jensen, L.H. Refinement of triclinic lysozyme. II. The method of stereochemically restrained least squares. Acta Crystallogr. B 46:63-69, 1990.
    • (1990) Acta Crystallogr. B , vol.46 , pp. 63-69
    • Ramanadham, M.1    Sieker, L.C.2    Jensen, L.H.3
  • 49
    • 0028001872 scopus 로고
    • X-ray structure of a monoclinic form of hen egg-while lysozyme crystallized at 313 K: Comparison of two independent molecules
    • Harata, K. X-ray structure of a monoclinic form of hen egg-while lysozyme crystallized at 313 K: Comparison of two independent molecules. Acta Crystallogr. D 50:250-257, 1994.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 250-257
    • Harata, K.1
  • 53
    • 0024362070 scopus 로고
    • On the attribution of binding energy in antigen-antibody complexes McPC603, D1.3, and HyHEL-5
    • Novotny, J., Bruccolery, R.E., Saul, F.E. On the attribution of binding energy in antigen-antibody complexes McPC603, D1.3, and HyHEL-5. Biochemistry 28:4735-4749, 1989.
    • (1989) Biochemistry , vol.28 , pp. 4735-4749
    • Novotny, J.1    Bruccolery, R.E.2    Saul, F.E.3
  • 54
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950, 1991.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 55
    • 10144251867 scopus 로고    scopus 로고
    • Ramanadham et al. 1987
    • Ramanadham et al. 1987.
  • 56
    • 0024292833 scopus 로고
    • Aromatic rings act as hydrogen bond acceptors
    • Levitt, M., Perutz, M.F. Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol. 201:751-754, 1988.
    • (1988) J. Mol. Biol. , vol.201 , pp. 751-754
    • Levitt, M.1    Perutz, M.F.2
  • 57
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5
    • Hibbits, K.A., Gill, D.S., Wilson, R.C. Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5. Biochemistry 33:3584-3590, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbits, K.A.1    Gill, D.S.2    Wilson, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.