Abstract
Background: Although infliximab has high efficacy in treating TNFα-associated diseases, the epitope on TNFα remains unclear. Results: The crystal structure of the TNFα in complex with the infliximab Fab is reported at a resolution of 2.6 Å. Conclusion: TNFα E-F loop plays a crucial role in the interaction. Significance: The structure may lead to understanding the mechanism of mAb anti-TNFα. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Liang, S., Dai, J., Hou, S., Su, L., Zhang, D., Guo, H., … Lou, Z. (2013). Structural basis for treating tumor necrosis factor α (TNFα)-associated diseases with the therapeutic antibody infliximab. Journal of Biological Chemistry, 288(19), 13799–13807. https://doi.org/10.1074/jbc.M112.433961
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