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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1107-1113 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of the Fab fragment of the murine monoclonal antibody A5B7, which is specific for carcinoembryonic antigen (CEA) a protein expressed on carcinoma cell surfaces, has been determined. The structure was solved by molecular replacement and has been refined to an R factor for 21.2% (all data 8–2.1 Å). The conformation of the hypervariable loops, which form the antigen binding site, are consistent with canonical loop predictions. Hypervariable loop H3 is unusual in surface exposing many hydrophobic groups at the expense of burying an aspartic acid in the protein core. Other regions of the structure that influence the conformation of the binding site are identified. This structure forms a basis for analysing the effects of amino-acid substitutions in both hypervariable and framework regions in engineering studies of the A5B7 antibody.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Gene 49 (1986), S. 53-60 
    ISSN: 0378-1119
    Keywords: Mung-bean-nuclease mapping ; inverted repeats ; operators ; recombinant DNA ; transcriptional regulation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0887-3585
    Keywords: protein ; antibody humanization ; quaternary structure ; complementarity-determining region ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The crystal structures of two pairs of Fab fragments have been determined. The pairs comprise both a murine and an engineered human form, each derived from the antitumor antibodies A5B7 and CTM01. Although antigen specificity is maintained within the pairs, antigen affinity varies. A comparison of the hypervariable loops for each pair of antibodies shows their structure has been well maintained in grafting, supporting the canonical loop model. Detailed structural analysis of the binding sites and domain arrangements for these antibodies suggests the differences in antigen affinity observed are likely to be due to inherent flexibility of the hypervariable loops and movements at the VL:VH domain interface. The four structures provide the first opportunity to study in detail the effects of protein engineering on specific antibodies. Proteins 29:161-171, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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