Thursday, July 11, 2013
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Structural analysis of
bovine complementarity-determining regions (CDRs) could guide the development
of new antibody libraries. Cows have distinct immunoglobulin features
including long CDRs and limited variable regions, and the molecular basis of
their antibody diversity is not well understood. A series of computational
and structural experiments demonstrated that these long CDRs can form
numerous disulfide bonds that generate structural diversity through folding
into unusual stalk- or knob-shaped structures. Next steps include
constructing libraries of cow antibodies to identify hits against potentially
LLC, which coauthored the study and was cofounded by Vaughn
Smider, is developing antibody screening platforms based on the technology.
Published online July 11, 2013
Patent applications filed;
unavailable for licensing
Wang, F. et al. Cell;
published online June 6, 2013;
Contact: Vaughn V. Smider, The Scripps Research Institute,
La Jolla, Calif.
Contact: Ian A. Wilson, same affiliation as above
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