In: PLOS ONE
8(4), e61953
[PDF, 2MB]
Abstract
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.
Dokumententyp: | Zeitschriftenartikel |
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Publikationsform: | Publisher's Version |
Fakultät: | Medizin |
Themengebiete: | 600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin und Gesundheit |
URN: | urn:nbn:de:bvb:19-epub-15347-7 |
ISSN: | 1932-6203 |
Sprache: | Englisch |
Dokumenten ID: | 15347 |
Datum der Veröffentlichung auf Open Access LMU: | 27. Mai 2013, 09:24 |
Letzte Änderungen: | 04. Nov. 2020, 12:56 |