Two-faced Fcab prevents polymerization with VEGF and reveals thermodynamics and the 2.15 Å crystal structure of the complex

Fcabs (Fc domain with antigen-binding sites) are promising novel therapeutics. By engineering of the C-terminal loops of the CH3 domains, 2 antigen binding sites can be inserted in close proximity. To elucidate the binding mode(s) between homodimeric Fcabs and small homodimeric antigens, the interac...

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Detaylı Bibliyografya
Yayımlandı:MAbs
Asıl Yazarlar: Lobner, Elisabeth, Humm, Anne-Sophie, Mlynek, Georg, Kubinger, Konstantin, Kitzmüller, Michael, Traxlmayr, Michael W., Djinović-Carugo, Kristina, Obinger, Christian
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Taylor & Francis 2017
Konular:
Report
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC5627596/
https://ncbi.nlm.nih.gov/pubmed/28816592
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1080/19420862.2017.1364825
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