4nux
From Proteopedia
(Difference between revisions)
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<StructureSection load='4nux' size='340' side='right' caption='[[4nux]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='4nux' size='340' side='right' caption='[[4nux]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4nux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUX OCA]. | + | <table><tr><td colspan='2'>[[4nux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NUX FirstGlance]. <br> |
| - | + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nux RCSB], [http://www.ebi.ac.uk/pdbsum/4nux PDBsum]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nux RCSB], [http://www.ebi.ac.uk/pdbsum/4nux PDBsum]</span></td></tr> | + | |
<table> | <table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/I17RA_HUMAN I17RA_HUMAN]] Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling.<ref>PMID:21993848</ref> <ref>PMID:19838198</ref> | [[http://www.uniprot.org/uniprot/I17RA_HUMAN I17RA_HUMAN]] Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling.<ref>PMID:21993848</ref> <ref>PMID:19838198</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:36, 24 September 2014
Structure of receptor A
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