1md6

<table><tr><td colspan='2'>[[1md6]] 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=1MD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MD6 FirstGlance]. <br>

</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=1md6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md6 OCA], [https://pdbe.org/1md6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1md6 RCSB], [https://www.ebi.ac.uk/pdbsum/1md6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1md6 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/I36RA_MOUSE I36RA_MOUSE]] Is a highly and a specific antagonist of the IL-1 receptor-related protein 2-mediated response to interleukin 1 family member 9 (IL1F9). Could constitute part of an independent signaling system analogous to interleukin-1 alpha (IL-1A), beta (IL-1B) receptor agonist and interleukin-1 receptor type I (IL-1R1), that is present in epithelial barriers and takes part in local inflammatory response (By similarity).

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== Publication Abstract from PubMed ==

Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studies give insights into how distinct receptor specificities can evolve within related cytokine families.

High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity.,Dunn EF, Gay NJ, Bristow AF, Gearing DP, O'Neill LA, Pei XY Biochemistry. 2003 Sep 23;42(37):10938-44. PMID:12974628<ref>PMID:12974628</ref>

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

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== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Dunn, E F]]

[[Category: Gay, N J]]

[[Category: Neill, L A.O]]

[[Category: Pei, X Y]]

[[Category: Immune system]]