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== | ==Crystal Structure of Human Interleukin-19== | ||
Interleukin-19 (IL-19) is a novel cytokine that was initially identified | <StructureSection load='1n1f' size='340' side='right'caption='[[1n1f]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1n1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1n1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1f OCA], [https://pdbe.org/1n1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1f RCSB], [https://www.ebi.ac.uk/pdbsum/1n1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IL19_HUMAN IL19_HUMAN] May play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n1/1n1f_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n1f ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Interleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. We determined the crystal structure of human recombinant IL-19 and refined it at 1.95-A resolution to an R-factor of 0.157. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle. On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines. | |||
Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.,Chang C, Magracheva E, Kozlov S, Fong S, Tobin G, Kotenko S, Wlodawer A, Zdanov A J Biol Chem. 2003 Jan 31;278(5):3308-13. Epub 2002 Oct 25. PMID:12403790<ref>PMID:12403790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1n1f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interleukin 3D structures|Interleukin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Chang C]] | ||
[[Category: Fong | [[Category: Fong S]] | ||
[[Category: Kotenko | [[Category: Kotenko S]] | ||
[[Category: Kozlov | [[Category: Kozlov S]] | ||
[[Category: Magracheva | [[Category: Magracheva E]] | ||
[[Category: Tobin | [[Category: Tobin G]] | ||
[[Category: Wlodawer | [[Category: Wlodawer A]] | ||
[[Category: Zdanov | [[Category: Zdanov A]] | ||
Latest revision as of 10:03, 30 October 2024
Crystal Structure of Human Interleukin-19Crystal Structure of Human Interleukin-19
Structural highlights
FunctionIL19_HUMAN May play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInterleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. We determined the crystal structure of human recombinant IL-19 and refined it at 1.95-A resolution to an R-factor of 0.157. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle. On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines. Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.,Chang C, Magracheva E, Kozlov S, Fong S, Tobin G, Kotenko S, Wlodawer A, Zdanov A J Biol Chem. 2003 Jan 31;278(5):3308-13. Epub 2002 Oct 25. PMID:12403790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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