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![[Figure 4]](dw5093fig4mag.jpg)
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Figure 4
Helix αC of IL-17RA SEFIR is key to function. (a) IL-17RA-deficient MEFs were reconstituted with empty vector and Myc-tagged mouse RA mutants by retroviral infection, after which the cells were treated with IL-17 for 10 min followed by immunoprecipitation with anti-Myc antibody and Western blot analysis with the indicated antibodies. The densities of Act1 bands from the immunocomplexes and whole cell lysate were quantified using ImageJ and their ratios were normalized with respect to the wild-type sample and shown as Act1 binding. (b) The same cells as in (a) were treated with IL-17 for 3 h. The abundances of cxcl1 mRNAs were measured by real-time RT-PCR and the induction (fold) of mRNA was calculated as the ratio of the amount of mRNA in the treated sample compared with that in the untreated sample. Data are means ± SEMs from three experiments. An asterisk indicates p < 0.05 (a difference from the wild-type sample). (c) The functionally defective mutations are located on the surface of helix αC. The IL-17RA SEFIR structure is shown in green as a surface representation. The surfaces of the human IL-17RA SEFIR structure corresponding to the five mouse mutation sites are colored magenta (M1; T480/N484/M485), yellow (M2; L458/L459), light pink (M3; R449/R452/Q456), orange (M4; E417/Q418/E422) and cyan (M5; V425/M426). The C-terminal end of helix αG (residue Tyr591) is shown in red. Note that Tyr591 is oriented in the same direction as the surface of helix αC. |
![[Figure 4]](dw5093fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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