Abstract
Background: Antibodies from alternative immune hosts provide insights into novel mechanisms of antibody diversity in restricted germ-line repertoires. Results: The high-resolution crystal structures of the first two chicken single chain antibodies (scFv) with prototypical binding sites are described. Conclusion: Chickens exhibit unique canonical classes in the CDRL1. Significance: Aves employ distinct mechanisms to generate diversity resulting in unique binding-site topologies. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Conroy, P. J., Law, R. H. P., Gilgunn, S., Hearty, S., Caradoc-Davies, T. T., Lloyd, G., … Whisstock, J. C. (2014). Reconciling the structural attributes of avian antibodies. Journal of Biological Chemistry, 289(22), 15384–15392. https://doi.org/10.1074/jbc.M114.562470
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