4nux

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nux OCA], [https://pdbe.org/4nux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nux RCSB], [https://www.ebi.ac.uk/pdbsum/4nux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nux ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Interleukin 17 (IL-17) cytokines play a crucial role in mediating inflammatory and autoimmune diseases. A unique intracellular signaling domain termed SEFIR is found within all IL-17 receptors (IL-17Rs) as well as the key adaptor protein Act1. SEFIR-mediated protein-protein interaction is a crucial step in IL-17 cytokine signaling. Here, the 2.3 A resolution crystal structure of the SEFIR domain of IL-17RA, the most commonly shared receptor for IL-17 cytokine signaling, is reported. The structure includes the complete SEFIR domain and an additional alpha-helical C-terminal extension, which pack tightly together to form a compact unit. Structural comparison between the SEFIR domains of IL-17RA and IL-17RB reveals substantial differences in protein topology and folding. The uniquely long insertion between strand betaC and helix alphaC in IL-17RA SEFIR is mostly well ordered, displaying a helix (alphaCC'ins) and a flexible loop (CC'). The DD' loop in the IL-17RA SEFIR structure is much shorter; it rotates nearly 90 degrees with respect to the counterpart in the IL-17RB SEFIR structure and shifts about 12 A to accommodate the alphaCC'ins helix without forming any knots. Helix alphaC was identified as critical for its interaction with Act1 and IL-17-stimulated gene expression. The data suggest that the heterotypic SEFIR-SEFIR association via helix alphaC is a conserved and signature mechanism specific for IL-17 signaling. The structure also suggests that the downstream motif of IL-17RA SEFIR together with helix alphaC could provide a composite ligand-binding surface for recruiting Act1 during IL-17 signaling.

Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved alpha-helix for Act1 binding and IL-17 signaling.,Zhang B, Liu C, Qian W, Han Y, Li X, Deng J Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1476-83. doi:, 10.1107/S1399004714005227. Epub 2014 Apr 30. PMID:24816115<ref>PMID:24816115</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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