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Volumn 259, Issue 5, 1996, Pages 957-969

Rearrangement of the former VL interface in the solution structure of a camelised, single antibody VH domain

Author keywords

Antibody engineering; Camel; Hydrophobicity; Immunoglobulin; NMR

Indexed keywords

IMMUNOGLOBULIN ANTIBODY; MUTANT PROTEIN;

EID: 0030604701     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0373     Document Type: Article
Times cited : (60)

References (38)
  • 5
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. The packing of variable domains
    • Chothia, C., Novotny, J., Bruccoleri, R. & Karplus, M. (1985). Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651-663.
    • (1985) J. Mol. Biol. , vol.186 , pp. 651-663
    • Chothia, C.1    Novotny, J.2    Bruccoleri, R.3    Karplus, M.4
  • 8
    • 0027953603 scopus 로고
    • Camelising human antibody fragments: NMR studies on VH domains
    • Davies, J. & Riechmann, L. (1994). Camelising human antibody fragments: NMR studies on VH domains. FEBS Letters, 339, 285-290.
    • (1994) FEBS Letters , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 9
    • 0029043683 scopus 로고
    • Antibody VH domains as small recognition units
    • Davies, J. & Riechmhann, L. (1995a). Antibody VH domains as small recognition units. Bio/Technology, 13, 475-479.
    • (1995) Bio/Technology , vol.13 , pp. 475-479
    • Davies, J.1    Riechmhann, L.2
  • 10
    • 0029562955 scopus 로고
    • An antibody VH domain with a lox-Cre site integrated into its coding region: Bacterial recombination within a single polypeptide chain
    • Davies, J. & Riechmann, L. (1995b). An antibody VH domain with a lox-Cre site integrated into its coding region: bacterial recombination within a single polypeptide chain. FEBS Letters, 377, 92-96.
    • (1995) FEBS Letters , vol.377 , pp. 92-96
    • Davies, J.1    Riechmann, L.2
  • 11
    • 0029746203 scopus 로고    scopus 로고
    • Single antibody domains as small recognition units: Design and in vitro antigen selection of camelised, human VH domains with improved protein stability
    • In the press
    • Davies, J. & Riechmann, L. (1996). Single antibody domains as small recognition units: design and in vitro antigen selection of camelised, human VH domains with improved protein stability. Protein Eng. 9. In the press.
    • (1996) Protein Eng. , pp. 9
    • Davies, J.1    Riechmann, L.2
  • 12
    • 0027053207 scopus 로고
    • On the multiple simultaneous superposition of molecular structures by rigid body transformation
    • Diamond, R. (1992). On the multiple simultaneous superposition of molecular structures by rigid body transformation. Protein Sci. 1, 1279-1287.
    • (1992) Protein Sci. , vol.1 , pp. 1279-1287
    • Diamond, R.1
  • 13
    • 0002855179 scopus 로고
    • Coordinate-based cluster-analysis
    • Diamond, R. (1995). Coordinate-based cluster-analysis. Acta Crystallog. sect. D, 51, 127-135.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 127-135
    • Diamond, R.1
  • 14
    • 0026468883 scopus 로고
    • Three-dimensional structure of an Fv from a human IgM immunoglobulin
    • Fan, Z.-C., Shan, L., Guddat, L. W., He, X.-M. & Gray, W. R. (1992). Three-dimensional structure of an Fv from a human IgM immunoglobulin. J. Mol. Biol. 228, 188-207.
    • (1992) J. Mol. Biol. , vol.228 , pp. 188-207
    • Fan, Z.-C.1    Shan, L.2    Guddat, L.W.3    He, X.-M.4    Gray, W.R.5
  • 18
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A., Serrano, L., Avron, B., Bycroft, M. & Fersht, A. R. (1990). Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 19
    • 0023643824 scopus 로고
    • Stereo assignment of side-chain protons and characterisation of torsion angles in Eglin c
    • Hyberts, S. G., Märki, W. & Wagner, G. (1987). Stereo assignment of side-chain protons and characterisation of torsion angles in Eglin c. Eur. J. Biochem. 164, 625-635.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Märki, W.2    Wagner, G.3
  • 21
    • 0026225733 scopus 로고
    • 13C-labeled protein using constant-time evolution
    • 13C-labeled protein using constant-time evolution. J. Biomol. NMR, 1, 299-304.
    • (1991) J. Biomol. NMR , vol.1 , pp. 299-304
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 22
    • 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. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0001339532 scopus 로고
    • Similarity of protein G and ubiquitin
    • Kraulis, P. J. (1991). Similarity of protein G and ubiquitin. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0028168145 scopus 로고
    • Sequence and structure of VH domains from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J. A. R. G. & Hamers, R. (1994). Sequence and structure of VH domains from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7, 1129-1135.
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.R.G.4    Hamers, R.5
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0023998438 scopus 로고
    • Determination of 3-dimensional structures of proteins by simulated annealing with interproton distance restraints - Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor-2
    • Nilges, M., Gronenborn, A. M., Brünger, A. T. & Clore, G. M. (1988). Determination of 3-dimensional structures of proteins by simulated annealing with interproton distance restraints - application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor-2. Protein Eng. 2, 27-38.
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 31
    • 0016763223 scopus 로고
    • Structural basis for the association of heavy and light chains and the relation of subgroups to the conformation of the active site of immunoglobulins
    • Poljak, R. J., Amzel, L. M., Chen, B. L., Phizackerley, R. P. & Saul, F. (1975). Structural basis for the association of heavy and light chains and the relation of subgroups to the conformation of the active site of immunoglobulins. Immunogenetics, 2, 393-394.
    • (1975) Immunogenetics , vol.2 , pp. 393-394
    • Poljak, R.J.1    Amzel, L.M.2    Chen, B.L.3    Phizackerley, R.P.4    Saul, F.5
  • 32
    • 0029365465 scopus 로고
    • Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain
    • Riechmann, L. & Davies, J. (1995). Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain. J. Biomol. NMR, 6, 141-152.
    • (1995) J. Biomol. NMR , vol.6 , pp. 141-152
    • Riechmann, L.1    Davies, J.2
  • 33
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J., Haberkorn, R. A. & Ruben, D. J. (1982). A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48, 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 34
    • 0001047001 scopus 로고
    • The subunits of purified rabbit antibody
    • Utsumi, S. & Karush, F. (1964). The subunits of purified rabbit antibody. Biochemistry, 3, 1329-1338.
    • (1964) Biochemistry , vol.3 , pp. 1329-1338
    • Utsumi, S.1    Karush, F.2
  • 36
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward, E. S., Güssow, D., Griffiths, A. D., Jones, P. T. & Winter, G. (1989). Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature, 341, 544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Güssow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.