메뉴 건너뛰기




Volumn 268, Issue 5, 1997, Pages 934-951

The rational construction of an antibody against cystatin: Lessons from the crystal structure of an artificial F(ab) fragment

Author keywords

Antigen binding; Computer modelling; Immunoglobulin; Protein engineering; X ray crystallography

Indexed keywords

ANTIBODY; CYSTATIN; IMMUNOGLOBULIN F(AB) FRAGMENT; TRYPTOPHAN;

EID: 0031584270     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1006     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0029161721 scopus 로고
    • Conformational similarity and systematic displacement of complementarity determining region loops in high resolution X-ray antibody structures
    • Bajorath J., Harris L., Novotny N. Conformational similarity and systematic displacement of complementarity determining region loops in high resolution X-ray antibody structures. J. Biol. Chem. 270:1995;22081-22084.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22081-22084
    • Bajorath, J.1    Harris, L.2    Novotny, N.3
  • 2
    • 0025151612 scopus 로고
    • Small rearrangements 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 of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature. 347:1990;483-485.
    • (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
  • 4
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., Turk V. The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7:1988;2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 5
    • 0028828994 scopus 로고
    • The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 Å resolution
    • Bossart-Whitaker P., Chang C. H. Y., Novotny J., Benjamin D. C., Sheriff S. The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 Å resolution. J. Mol. Biol. 253:1995;559-575.
    • (1995) J. Mol. Biol. , vol.253 , pp. 559-575
    • Bossart-Whitaker, P.1    Chang, C.H.Y.2    Novotny, J.3    Benjamin, D.C.4    Sheriff, S.5
  • 6
    • 0027971497 scopus 로고
    • Three-dimensional structure of the free and the antigen-complexed Fab from the monoclonal anti-lysozyme antibody D44.1
    • Braden C. B., Souchon H., Eisele J. L., Bentley G. A., Bhat T. N., Navaza J., Poljak R. J. Three-dimensional structure of the free and the antigen-complexed Fab from the monoclonal anti-lysozyme antibody D44.1. J. Mol. Biol. 243:1994;767-781.
    • (1994) J. Mol. Biol. , vol.243 , pp. 767-781
    • Braden, C.B.1    Souchon, H.2    Eisele, J.L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 7
    • 0029870875 scopus 로고    scopus 로고
    • Crystal structure of the complex of the variable domain of antibody D1.3 and turkey egg white lysozyme: A novel conformational change in antibody CDR-L3 selects for antigen
    • Braden C. B., Fields B. A., Ysern X., Goldbaum F. A., Dall'Acqua W., Schwarz P. F., Poljak R. J., Mariuzza R. A. Crystal structure of the complex of the variable domain of antibody D1.3 and turkey egg white lysozyme: a novel conformational change in antibody CDR-L3 selects for antigen. J. Mol. Biol. 257:1996;889-894.
    • (1996) J. Mol. Biol. , vol.257 , pp. 889-894
    • Braden, C.B.1    Fields, B.A.2    Ysern, X.3    Goldbaum, F.A.4    Dall'Acqua, W.5    Schwarz, P.F.6    Poljak, R.J.7    Mariuzza, R.A.8
  • 8
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger A. T. Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallog. sect. A. 46:1990;46-57.
    • (1990) Acta Crystallog. Sect. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 9
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. T. Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 335:1992a;472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 11
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free r value. Methods and applications
    • Brünger A. T. Assessment of phase accuracy by cross validation: the free r value. Methods and applications. Acta Crystallog. sect. D. 49:1993;24-36.
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 24-36
    • Brünger, A.T.1
  • 12
    • 0023278330 scopus 로고
    • Canonical structure for the hypervariable regions of immunoglobulins
    • Chothia C., Lesk A. M. Canonical structure for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196:1987;901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 15
    • 0021107965 scopus 로고
    • Solvent accessible surfaces of proteins and nucleic acids
    • Connolly M. L. Solvent accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 17
    • 0026319774 scopus 로고
    • Recognition of a cell-surface oligosaccharide of pathogenicSalmonella
    • Cygler M., Rose D. R., Bundle D. R. Recognition of a cell-surface oligosaccharide of pathogenicSalmonella. Science. 253:1991;442-445.
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 21
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 22
    • 0027768859 scopus 로고
    • Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy
    • Engh R., Dieckmann T., Bode W., Auerswald E. A., Turk V., Huber R., Oschkinat H. Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy. J. Mol. Biol. 234:1993;1060-1069.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1060-1069
    • Engh, R.1    Dieckmann, T.2    Bode, W.3    Auerswald, E.A.4    Turk, V.5    Huber, R.6    Oschkinat, H.7
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in the models
    • Jones T. A., Zou J.-Y., Cowan S. W. Improved methods for building protein models in electron density maps and the location of errors in the models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 32
    • 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. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule KOL and its antigen binding fragment at 3.0 Å and 1.9 Å resolution
    • Marquart M., Deisenhofer J., Huber R., Palm W. Crystallographic refinement and atomic models of the intact immunoglobulin molecule KOL and its antigen binding fragment at 3.0 Å and 1.9 Å resolution. J. Mol. Biol. 141:1980;396-391.
    • (1980) J. Mol. Biol. , vol.141 , pp. 396-391
    • Marquart, M.1    Deisenhofer, J.2    Huber, R.3    Palm, W.4
  • 34
    • 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
  • 36
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan E. A. Anatomy of the antibody molecule. Mol. Immunol. 31:1994;169-217.
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 38
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder J. W., Richards F. M. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193:1987;775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 41
    • 0029016430 scopus 로고
    • Protein design - Novel metal binding sites
    • Regan L. Protein design - novel metal binding sites. Trends Biochem. Sci. 20:1995;280-285.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 43
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603. An X-ray study at 2.7 Å
    • Satow Y., Cohen G. H., Padlan E. A., Davies D. R. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray study at 2.7 Å J. Mol. Biol. 190:1986;593-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 44
    • 0026706824 scopus 로고
    • Crystal structure of human immunoglobulin fragment Fab New refined at 2.0 Å resolution
    • Saul A. F., Poljak R. J. Crystal structure of human immunoglobulin fragment Fab New refined at 2.0 Å resolution. Proteins: Struct. Funct. Genet. 14:1992;363-371.
    • (1992) Proteins: Struct. Funct. Genet. , vol.14 , pp. 363-371
    • Saul, A.F.1    Poljak, R.J.2
  • 45
    • 0029609390 scopus 로고
    • Fermenter production of an artificial Fab fragment, rationally designed for the antigen cystatin, and its optimized crystallization through constant domain shuffling
    • Schiweck W., Skerra A. Fermenter production of an artificial Fab fragment, rationally designed for the antigen cystatin, and its optimized crystallization through constant domain shuffling. Proteins: Struct. Funct. Genet. 23:1995;561-565.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 561-565
    • Schiweck, W.1    Skerra, A.2
  • 46
    • 0030220473 scopus 로고    scopus 로고
    • A Zn (II)-binding site engineered into retinol-binding protein exhibits metal-ion specifity and allows highly specific affinity purification with a newly designed metal ligand
    • Schmidt A. M., Müller H. N., Skerra A. A Zn (II)-binding site engineered into retinol-binding protein exhibits metal-ion specifity and allows highly specific affinity purification with a newly designed metal ligand. Chem. Biol. 3:1996;645-653.
    • (1996) Chem. Biol. , vol.3 , pp. 645-653
    • Schmidt, A.M.1    Müller, H.N.2    Skerra, A.3
  • 47
    • 0030604686 scopus 로고    scopus 로고
    • X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form
    • Sheriff S., Chang C.-Y. Y., Jeffrey P. D., Bajorath J. X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form. J. Mol. Biol. 259:1996;938-946.
    • (1996) J. Mol. Biol. , vol.259 , pp. 938-946
    • Sheriff, S.1    Chang, C.-Y.Y.2    Jeffrey, P.D.3    Bajorath, J.4
  • 49
    • 0026631064 scopus 로고
    • Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
    • Steipe B., Plückthun A., Huber R. Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant. J. Mol. Biol. 225:1992;739-753.
    • (1992) J. Mol. Biol. , vol.225 , pp. 739-753
    • Steipe, B.1    Plückthun, A.2    Huber, R.3
  • 52
    • 0002738505 scopus 로고
    • A year in the life of the immunoglobulin superfamily
    • Williams A. F. A year in the life of the immunoglobulin superfamily. Immunol. Today. 8:1987;298-303.
    • (1987) Immunol. Today , vol.8 , pp. 298-303
    • Williams, A.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.