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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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מידע ביבליוגרפי
הוצא לאור ב:	MAbs
Main Authors:	Lobner, Elisabeth, Humm, Anne-Sophie, Mlynek, Georg, Kubinger, Konstantin, Kitzmüller, Michael, Traxlmayr, Michael W., Djinović-Carugo, Kristina, Obinger, Christian
פורמט:	Artigo
שפה:	Inglês
יצא לאור:	Taylor & Francis 2017
נושאים:	Report
גישה מקוונת:	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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Two-faced Fcab prevents polymerization with VEGF and reveals thermodynamics and the 2.15 Å crystal structure of the complex

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