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Publication Detail
Structural models for carcinoembryonic antigen and its complex with the single-chain Fv antibody molecule MFE23
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Publication Type:Journal article
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Publication Sub Type:Article
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Authors:Boehm MK, Perkins SJ
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Publication date:2000
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Pagination:11, 16
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Journal:Federation of European Biochemical Societies Letters
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Volume:475
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Issue:1
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Print ISSN:0014-5793
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Keywords:0 (Carcinoembryonic Antigen), 0 (Immunoglobulin Fragments), 0 (immunoglobulin Fv), AFFINITIES, affinity, Amino Acid Sequence, antibodies, Antibody, ANTIGEN, biochemical, Biochemistry, biology, Carcinoembryonic Antigen, chemistry, COMPLEX, COMPLEXES, CRYSTAL, CRYSTAL STRUCTURE, domain, HIGH-AFFINITY, Immunoglobulin Fragments, MED, metabolism, model, MODELS, Models, Molecular, Molecular, Molecular Biology, Molecular Sequence Data, N-terminal, oligosaccharides, Protein Binding, Protein Conformation, scattering, Structure, SURFACE, UK, Amino Acid Sequence
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Author URL:
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Addresses:Department of Biochemistry and Molecular Biology, Royal Free and University College Medical School, University College London, London, UK
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Notes:UI - 20314459 LA - eng RN - 0 (Carcinoembryonic Antigen) RN - 0 (Immunoglobulin Fragments) RN - 0 (immunoglobulin Fv) PT - Journal Article DA - 20000724 IS - 0014-5793 SB - IM CY - NETHERLANDS JC - EUH
Abstract
MFE23 is a single chain Fv antibody that has a high affinity for carcinoembryonic antigen (CEA). A full homology model for CEA based on V-type, I-type and C2-type immunoglobulin folds, 28 oligosaccharides and the interdomain angle of CD2 was validated using solution scattering data. The superimposition of the intermolecular contacts observed in our recent crystal structure of MFE23 with the N-terminal domain of CEA permitted the MFE23-CEA complex to be modelled. Good surface and electrostatic complementarity and carbohydrate-unhindered access of MFE23 with the indentation between the first two CEA domains was observed. The model is supported by biochemical data and provides insight on the high affinity of MFE23 for CEA
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