Structural Characterisation Reveals Mechanism of IL-13-Neutralising Monoclonal Antibody Tralokinumab as Inhibition of Binding to IL-13Rα1 and IL-13Rα2

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Structural Characterisation Reveals Mechanism of IL-13-Neutralising Monoclonal Antibody Tralokinumab as Inhibition of Binding to IL-13Rα1 and IL-13Rα2

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作者：B. Popovic¹ ; ^{popovicb@medimmune.com} ; J. Breed² ; D.G. Rees¹ ; M.J. Gardener¹ ; L.M.K. Vinall¹ ; B. Kemp¹ ; J. Spooner¹ ; J. Keen¹ ; R. Minter¹ ; F. Uddin³ ; G. Colice⁴ ; T. Wilkinson¹ ; T. Vaughan¹ ; R.D. May⁵
关键词：IL ; interleukin ; Th2 ; T helper type 2 ; PDB ; Protein Data Bank ; VH ; variable heavy ; VL ; variable light region ; CDR ; complementary-determining region ; FW ; framework ; PBS ; phosphate-buffered saline ; HPLC-SEC ; high-performance liquid chromatography&ndash ; size-exclusion chromatography ; HTRF ; homogeneous time resolved fluorescence
刊名：Journal of Molecular Biology
出版年：2017
出版时间：20 January 2017
年：2017
卷：429
期：2
页码：208-219
全文大小：2089 K
卷排序：429

文摘

IL-13 has been shown to drive key disease mechanisms in asthma. Anti-IL-13 antibody tralokinumab has a dissociation constant of 58 pM. Tralokinumab prevents binding IL-13 to IL-13Rα1 and IL-13Rα2.