Small rearrangements in structures of Fv and Fab fragments of antibody D 1.3 on antigen binding

• Published in: Nature (London) Vol. 347; no. 6292; pp. 483 - 485
• Main Authors: Bhat, T. N, Bentley, G. A, Fischmann, T. O, Boulot, G, Poljak, R. J
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 04-10-1990
• Subjects: Antigens; Binding; Chains; Deformation; Domains; Fragments; Hydrogen; Hydrogen bonding; Hydrogen bonds; Immunoglobulins; Immunology; Monoclonal antibodies; Organic chemistry; Protein engineering; Therapeutic applications; United States > US
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/347483a0

THE potential use of monoclonal antibodies in immunological, chemical and clinical applications has stimulated the protein engineering and expression of Fv fragments'^8, which are heterodimers consisting of the light and heavy chain variable domains (Vl and Vh) of antibodies. The Ca positions of the HEL moieties of the two complexes superpose (excluding residues 100-104 in the deformed loop) with an r.m.s. deviation of 0.39 Å. To study the effect of antigen binding on FvD1.3 and FabD1.3, comparisons were made between the free FvD1.3 and the antigen-bound FvD1.3 and FabD1.3 structures (Table 2 and Fig. 2). [...]a His residue would not fit into the cavity occupied by the side chain of Gin 121. [...]the replacement His would make at most one hydrogen bond instead of the three hydrogen bonds made by the side chain of Gin 121 (Fig. 1, and Table 1).