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Publication Abstract from PubMed

Bispecific antibodies are considered as a promising class of future biotherapeutic molecules. They comprise binding specificities for two different antigens, which may provide additive or synergistic modes of action. There is a wide variety of design alternatives for such bispecific antibodies, including the "CrossMab" format. CrossMabs contain a domain crossover in one of the antigen-binding (Fab) parts, together with the "knobs-and-holes" approach, to enforce the correct assembly of four different polypeptide chains into an IgG-like bispecific antibody. We determined the crystal structure of a hAng-2-binding Fab in its crossed and uncrossed form and show that CH1-CL-domain crossover does not induce significant perturbations of the structure and has no detectable influence on target binding.

Crystal structure of an anti-Ang2 CrossFab demonstrates complete structural and functional integrity of the variable domain.,Fenn S, Schiller CB, Griese JJ, Duerr H, Imhof-Jung S, Gassner C, Moelleken J, Regula JT, Schaefer W, Thomas M, Klein C, Hopfner KP, Kettenberger H PLoS One. 2013 Apr 17;8(4):e61953. doi: 10.1371/journal.pone.0061953. Print 2013. PMID:23613981^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.