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Volumn 3, Issue 9, 1996, Pages 803-811

Crystal structure of a camel single-domain V(H) antibody fragment in complex with lysozyme

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; LYSOZYME;

EID: 0029764444     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0996-803     Document Type: Article
Times cited : (446)

References (58)
  • 1
    • 0025978976 scopus 로고
    • Man-made antibodies
    • Winter, G. & Milstein, C. Man-made antibodies. Mature 349, 293-299 (1991).
    • (1991) Mature , vol.349 , pp. 293-299
    • Winter, G.1    Milstein, C.2
  • 3
    • 0026270455 scopus 로고
    • The minimal antigen-binding fragment of antibodies-Fv fragment
    • Givol, D. The minimal antigen-binding fragment of antibodies-Fv fragment. Molec. Immunol. 28, 1379-1386 (1991).
    • (1991) Molec. Immunol. , vol.28 , pp. 1379-1386
    • Givol, D.1
  • 4
    • 0026468883 scopus 로고
    • Three-dimensional structure of an Fv from a human IgM immunoglobulin
    • Fan, Z. et al. Three-dimensional structure of an Fv from a human IgM immunoglobulin. J. Mol. Biol. 228, 188-207 (1992).
    • (1992) J. Mol. Biol. , vol.228 , pp. 188-207
    • Fan, Z.1
  • 5
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E.A. Anatomy of the antibody molecule. Molec. Immunol. 31, 169-217 (1994).
    • (1994) Molec. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 6
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in E. coli
    • Skerra, A. & Plückthun, A. Assembly of a functional immunoglobulin Fv fragment in E. coli. Science. 240, 1038-1041 (1988).
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Plückthun, A.2
  • 7
    • 0027312336 scopus 로고
    • Bacterial expression of immunoglobulin fragments
    • Skerra, A. Bacterial expression of immunoglobulin fragments. Curr. Opin. Immunol. 5, 256-262 (1993).
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 256-262
    • Skerra, A.1
  • 8
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv fragments
    • Glockshuber, R., Malia, M., Pfitzinger, I. & Plückthun, A. A comparison of strategies to stabilize immunoglobulin Fv fragments, Biochemistry. 29, 1362-1367 (1990).
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Plückthun, A.4
  • 9
    • 0028275293 scopus 로고
    • Design of interchain disulfide bonds in the framework region of the Fv fragment of the monoclonal antibody B3
    • Jung, S., Pastan, I. & Lee, B. Design of interchain disulfide bonds in the framework region of the Fv fragment of the monoclonal antibody B3. Proteins Struct. Funct. Genet. 19, 35-47 (1994).
    • (1994) Proteins Struct. Funct. Genet. , vol.19 , pp. 35-47
    • Jung, S.1    Pastan, I.2    Lee, B.3
  • 10
    • 0024293979 scopus 로고
    • Single chain antigen binding proteins
    • Bird, R.E. et al. Single chain antigen binding proteins. Science. 241, 423-426 (1988).
    • (1988) Science , vol.241 , pp. 423-426
    • Bird, R.E.1
  • 11
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from E. coli
    • Ward, E.S., Gûssow, O, Griffiths, A.D., Jones, P.T. & Winter, G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from E. coli. Nature 341, 544-546 (1989).
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gûssow, O.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 12
    • 0027310612 scopus 로고
    • Naturally occurring antibodies devoid of light chains
    • Hamers-Casterman, C. et al. Naturally occurring antibodies devoid of light chains. Nature 363, 446-448 (1993).
    • (1993) Nature , vol.363 , pp. 446-448
    • Hamers-Casterman, C.1
  • 13
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J.A. & Hamers, R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Prot. Engng. 7, 1129-1135 (1994).
    • (1994) Prot. Engng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 14
    • 0027953603 scopus 로고
    • Camelising human antibody fragments: NMR studies on VH domains
    • Davies, J. & Riechmann, L Camelising human antibody fragments: NMR studies on VH domains. FEBS Letters. 339, 285-290 (1994).
    • (1994) FEBS Letters , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 15
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. The packing of variable domains
    • Chothia, C., Novotny, J., Bruccoleri, R. & Karplus, M. Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651-663 (1985).
    • (1985) J. Mol. Biol. , vol.186 , pp. 651-663
    • Chothia, C.1    Novotny, J.2    Bruccoleri, R.3    Karplus, M.4
  • 18
    • 0029043683 scopus 로고
    • Antibody VH domains as small recognition units
    • Davies, J. & Riechmann, L. Antibody VH domains as small recognition units. Bio/Technology. 13, 475-479 (1995).
    • (1995) Bio/Technology , vol.13 , pp. 475-479
    • Davies, J.1    Riechmann, L.2
  • 19
    • 0023447105 scopus 로고
    • Three-dimensional structure of an antibody-antigen complex
    • Sheriff, S. et al. Three-dimensional structure of an antibody-antigen complex. Proc. Natl. Acad. Sci. USA 84, 8075-8079 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8075-8079
    • Sheriff, S.1
  • 20
    • 0030047926 scopus 로고    scopus 로고
    • Refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg-white lysozyme
    • Cohen, G.H., Sheriff, S. & Davies, D.R. Refined structure of the monoclonal antibody HyHEL-5 with its antigen hen egg-white lysozyme. Acta Crystallogr. D52, 315-326 (1996)..
    • (1996) Acta Crystallogr. , vol.D52 , pp. 315-326
    • Cohen, G.H.1    Sheriff, S.2    Davies, D.R.3
  • 22
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antibody-antigen complex at 2.8 Å resolution
    • Amit, A.G., Mariuzza, R.A., Phillips, S.E. & Poljak, R.J. Three-dimensional structure of an antibody-antigen 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.3    Poljak, R.J.4
  • 23
    • 0028014642 scopus 로고
    • Bound water molecules and conformational stabilization help mediate an antigen-antibody association
    • Bhat, T.N. et al. Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl. Acad. Sci. USA 91, 1089-1093 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1089-1093
    • Bhat, T.N.1
  • 24
    • 0027203779 scopus 로고
    • Three dimensional structure of a heteroclinic antigen-antibody cross-reaction complex
    • Chitarra, V. et al. Three dimensional structure of a heteroclinic antigen-antibody cross-reaction complex. Proc. Natl. Acad. Sci. USA 90, 7711-7715 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7711-7715
    • Chitarra, V.1
  • 25
    • 0027971497 scopus 로고
    • Three dimensional structures of the free and the antigen-complexed Fab form monoclonal anti-lysozyme antibody D44.1
    • Braden, B.C. et al. Three dimensional structures of the free and the antigen-complexed Fab form 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
  • 26
    • 0343055582 scopus 로고
    • Structure of an antibody-antigen complex: Crystal structure of the HyHEL-10 Fab-lysozyme complex
    • Padlan, E.A. et al. Structure of an antibody-antigen complex: Crystal structure of the HyHEL-10 Fab-lysozyme complex. Proc. Natl. Acad. Sci. USA 86, 5938-5942 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5938-5942
    • Padlan, E.A.1
  • 27
    • 0028978247 scopus 로고
    • Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea-fowl lysozyme
    • Lescar, J. et.al. Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea-fowl lysozyme. J. Biol. Chem. 270, 18067-18076 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18067-18076
    • Lescar, J.1
  • 29
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies, D.R. & Cohen, G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 93, 7-12 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 30
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab), heavy and light chains
    • Hoogenboom, H.R. et al. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab), heavy and light chains. Nucl. Acids Res. 19, 4133-4137 (1991).
    • (1991) Nucl. Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1
  • 32
    • 0021964141 scopus 로고
    • Measurement of the true affinity constant in solution of antigenantibody complexes by enzyme linked immunosorbent assay
    • Friguet, B., Chaffotte, A.F., Djavadi-Ohaniance, L.D. & Goldberg, M.E. Measurement of the true affinity constant in solution of antigenantibody complexes by enzyme linked immunosorbent assay. J. Immunol. Meths. 77, 305-319 (1985).
    • (1985) J. Immunol. Meths. , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.D.3    Goldberg, M.E.4
  • 33
    • 0028001872 scopus 로고
    • X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules
    • Harata, K. X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules. Acta Crystallogr. D50, 250-257 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 250-257
    • Harata, K.1
  • 35
    • 2642648459 scopus 로고
    • The outline structure of the T-cell αβ receptor
    • Chothia, C., Boswell, D.R. & Lesk, A.M. The outline structure of the T-cell αβ receptor. EMBO J. 7, 3745-3755 (1988).
    • (1988) EMBO J. , vol.7 , pp. 3745-3755
    • Chothia, C.1    Boswell, D.R.2    Lesk, A.M.3
  • 36
    • 0026592314 scopus 로고
    • Immunoglobulin VH clan and family identity predicts variable domain structure and may influence antigen binding
    • Kirkham, P.M., Mortari, F., Newton, J.A. & Schroeder, H.W. Jr. Immunoglobulin VH clan and family identity predicts variable domain structure and may influence antigen binding. EMBO J. 11, 603-609 (1992).
    • (1992) EMBO J. , vol.11 , pp. 603-609
    • Kirkham, P.M.1    Mortari, F.2    Newton, J.A.3    Schroeder Jr., H.W.4
  • 37
    • 0026788298 scopus 로고
    • Structural repertoire of human VH segments
    • Chothia, C. et al. Structural repertoire of human VH segments. J. Mol. Biol. 227, 799-817 (1992).
    • (1992) J. Mol. Biol. , vol.227 , pp. 799-817
    • Chothia, C.1
  • 38
    • 0027452952 scopus 로고
    • Structural patterns at residue positions 9, 18, 67, and 82 in the VH framework regions of human and murine immunoglobulins
    • Saul, F.A. & Poljak, R.J. Structural patterns at residue positions 9, 18, 67, and 82 in the VH framework regions of human and murine immunoglobulins. J. Mol. Biol. 230, 15-20 (1993).
    • (1993) J. Mol. Biol. , vol.230 , pp. 15-20
    • Saul, F.A.1    Poljak, R.J.2
  • 39
    • 0030604701 scopus 로고    scopus 로고
    • Rearrangement of the former VL interface in the solution structure of a camelised, single domain VH antibody
    • Riechmann, L. Rearrangement of the former VL interface in the solution structure of a camelised, single domain VH antibody. J. Mol. Biol. 259, 957-969 (1996).
    • (1996) J. Mol. Biol. , vol.259 , pp. 957-969
    • Riechmann, L.1
  • 40
    • 0024844388 scopus 로고
    • Conformations of immunoglobulin hypervariable regions
    • Chothia, C. et al. Conformations of immunoglobulin hypervariable regions. Nature 342, 877-883 (1989).
    • (1989) Nature , vol.342 , pp. 877-883
    • Chothia, C.1
  • 41
    • 0025063143 scopus 로고
    • Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins
    • Tramontano, A., Chothia, C. & Lesk, A.M. Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins. J. Mol. Biol. 215, 175-182 (1990).
    • (1990) J. Mol. Biol. , vol.215 , pp. 175-182
    • Tramontano, A.1    Chothia, C.2    Lesk, A.M.3
  • 42
    • 0028676261 scopus 로고
    • Structural conservation of hypervariable regions in immunoglobulins evolution
    • Barré, S., Greenberg, A.S., Flajnik, M.F. & Chothia, C. Structural conservation of hypervariable regions in immunoglobulins evolution. Nature Struct. Biology 1, 915-920 (1994).
    • (1994) Nature Struct. Biology , vol.1 , pp. 915-920
    • Barré, S.1    Greenberg, A.S.2    Flajnik, M.F.3    Chothia, C.4
  • 43
    • 0026785856 scopus 로고
    • The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops
    • Tomlinson, I.M., Walter, G., Marks, J.D., Llewelyn, M.B. & Winter, G. The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops. J. Mol. Biol. 227, 776-798 (1992).
    • (1992) J. Mol. Biol. , vol.227 , pp. 776-798
    • Tomlinson, I.M.1    Walter, G.2    Marks, J.D.3    Llewelyn, M.B.4    Winter, G.5
  • 44
    • 0028327101 scopus 로고
    • Crystal structure of the principal neutralization site of HIV-1
    • Ghiara, J.B., Stura, E.A., Stanfield, L., Profy, A.T. & Wilson, I.A. Crystal structure of the principal neutralization site of HIV-1. Science 264, 82-85 (1994).
    • (1994) Science , vol.264 , pp. 82-85
    • Ghiara, J.B.1    Stura, E.A.2    Stanfield, L.3    Profy, A.T.4    Wilson, I.A.5
  • 47
    • 0028877602 scopus 로고
    • Structural features of the reactions between antibodies and protein antigens
    • Braden, B.C. & Poljak, R.J. Structural features of the reactions between antibodies and protein antigens. FASEB J. 9, 9-16 (1995).
    • (1995) FASEB J. , vol.9 , pp. 9-16
    • Braden, B.C.1    Poljak, R.J.2
  • 48
    • 0028103275 scopus 로고
    • All CCP4 software 'The CCP4 Suite': Programs for protein crystallography
    • All CCP4 software The CCP4 Suite': Programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 49
    • 0015222647 scopus 로고
    • The interpretation of protein structure: Estimation of static accessibility
    • Lee, B. & Richards, F.M. The interpretation of protein structure: estimation of static accessibility. J. Mol. Biol. 55, 379-400 (1971).
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 50
    • 0028819752 scopus 로고
    • Turning lysozyme upside down
    • Kirby, A.J. Turning lysozyme upside down. Nature Struct. Biology 2, 923-925 (1995).
    • (1995) Nature Struct. Biology , vol.2 , pp. 923-925
    • Kirby, A.J.1
  • 51
    • 0025818823 scopus 로고
    • Protein antigenicity: A thermodynamic approach
    • Novotny, J. Protein antigenicity: a thermodynamic approach. Molec. Immunol. 28, 201-207 (1991).
    • (1991) Molec. Immunol. , vol.28 , pp. 201-207
    • Novotny, J.1
  • 52
    • 85027633237 scopus 로고
    • Crystal orientation and X ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt, A. & Plugrath, 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
    • Messerschmidt, A.1    Plugrath, J.W.2
  • 54
    • 84889120137 scopus 로고
    • Improved method 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 method for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 55
    • 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. 335, 472-475 (1992).
    • (1992) Nature , vol.335 , pp. 472-475
    • Brünger, A.T.1
  • 56
    • 0000243829 scopus 로고
    • PROCHECK-A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK-A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 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
  • 58
    • 0028057108 scopus 로고
    • RASTER 3D version 2.0 a program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E. RASTER 3D version 2.0 a program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2


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