This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3vbc

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal Structure of iL-17 receptor B SEFIR domain

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vbc"

@@ Line 3: / Line 3: @@
 <StructureSection load='3vbc' size='340' side='right'caption='[[3vbc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBC FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Il17rb, Evi27, Il17br ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=3vbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbc OCA], [https://pdbe.org/3vbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vbc RCSB], [https://www.ebi.ac.uk/pdbsum/3vbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vbc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/I17RB_MOUSE I17RB_MOUSE]] Receptor for the proinflammatory cytokines IL17B and IL17E. May play a role in controlling the growth and/or differentiation of hematopoietic cells.
+[https://www.uniprot.org/uniprot/I17RB_MOUSE I17RB_MOUSE] Receptor for the proinflammatory cytokines IL17B and IL17E. May play a role in controlling the growth and/or differentiation of hematopoietic cells.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-IL-17 cytokines play a crucial role in a variety of inflammatory and autoimmune diseases. They signal through heterodimeric receptor complexes consisting of members of IL-17R family. A unique intracellular signaling domain was identified within all IL-17Rs, termed similar expression to fibroblast growth factor genes and IL-17R (SEFIR). SEFIR is also found in NF-kappaB activator 1 (Act1), an E3 ubiquitin ligase, and mediates its recruitment to IL-17Rs. In this study, to our knowledge, we report the structure of the first SEFIR domain from IL-17RB at 1.8A resolution. SEFIR displays a five-stranded parallel beta-sheet that is wrapped by six helices. Site-directed mutagenesis on IL-17RB identified helix alphaC as being critical for its interaction with Act1 and IL-25 (IL-17E) signaling. Using the current SEFIR structure as a template, the key functional residues in Act1 are also mapped as part of helix alphaC, which is conserved in IL-17RA and RC, suggesting this helix as a common structural signature for heterotypic SEFIR-SEFIR association. In contrast, helix alphaB' is important for homodimerization of Act1, implicating a dual ligand-binding model for SEFIR domain, with distinct structural motifs participating in either homotypic or heterotypic interactions. Furthermore, although the IL-17RB-SEFIR structure resembles closest to the Toll/IL-1R domain of TLR10 with low sequence homology, substantial differences were observed at helices alphaC, alphaD, and DD' loop. To our knowledge, this study provides the first structural view of the IL-17R intracellular signaling, unraveling the mechanism for the specificity of SEFIR versus Toll/IL-1R domain in their respective signaling pathways.
-Crystal Structure of IL-17 Receptor B SEFIR Domain.,Zhang B, Liu C, Qian W, Han Y, Li X, Deng J J Immunol. 2013 Mar 1;190(5):2320-6. doi: 10.4049/jimmunol.1202922. Epub 2013 Jan, 25. PMID:23355738<ref>PMID:23355738</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3vbc" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Deng, J]]
+[[Category: Deng J]]
-[[Category: Li, X]]
+[[Category: Li X]]
-[[Category: Liu, C]]
+[[Category: Liu C]]
-[[Category: Zhang, B]]
+[[Category: Zhang B]]
-[[Category: Autoimmune]]
-[[Category: Cytokine]]
-[[Category: Immune system]]
-[[Category: Inflammatory]]
-[[Category: Interleukin 17]]
-[[Category: Receptor]]
-[[Category: Sefir]]

3vbc

From Proteopedia

Current revision

Crystal Structure of iL-17 receptor B SEFIR domain

Structural highlights

Function

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox