2r3z: Difference between revisions
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==Crystal structure of mouse IP-10== | ==Crystal structure of mouse IP-10== | ||
<StructureSection load='2r3z' size='340' side='right' caption='[[2r3z]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2r3z' size='340' side='right'caption='[[2r3z]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2r3z]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2r3z]] is a 4 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=2R3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R3Z FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o7y|1o7y]], [[1o7z|1o7z]], [[1o80|1o80]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o7y|1o7y]], [[1o7z|1o7z]], [[1o80|1o80]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cxcl10, Crg2, Ifi10, Inp10, Scyb10 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cxcl10, Crg2, Ifi10, Inp10, Scyb10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r3z OCA], [https://pdbe.org/2r3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r3z RCSB], [https://www.ebi.ac.uk/pdbsum/2r3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r3z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CXL10_MOUSE CXL10_MOUSE]] In addition to its role as a proinflammatory cytokine, may participate in T-cell effector function and perhaps T-cell development. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[C-X-C motif chemokine|C-X-C motif chemokine]] | *[[C-X-C motif chemokine 3D structures|C-X-C motif chemokine 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Acharya, K R]] | [[Category: Acharya, K R]] | ||
Revision as of 07:13, 2 July 2021
Crystal structure of mouse IP-10Crystal structure of mouse IP-10
Structural highlights
Function[CXL10_MOUSE] In addition to its role as a proinflammatory cytokine, may participate in T-cell effector function and perhaps T-cell development. 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 PubMedInterferon-gamma-inducible protein (IP-10) belongs to the CXC class of chemokines and plays a significant role in the pathophysiology of various immune and inflammatory responses. It is also a potent angiostatic factor with antifibrotic properties. The biological activities of IP-10 are exerted by interactions with the G-protein-coupled receptor CXCR3 expressed on Th1 lymphocytes. IP-10 thus forms an attractive target for structure-based rational drug design of anti-inflammatory molecules. The crystal structure of mouse IP-10 has been determined and reveals a novel tetrameric association. In the tetramer, two conventional CXC chemokine dimers are associated through their N-terminal regions to form a 12-stranded elongated beta-sheet of approximately 90 A in length. This association differs significantly from the previously studied tetramers of human IP-10, platelet factor 4 and neutrophil-activating peptide-2. In addition, heparin- and receptor-binding residues were mapped on the surface of IP-10 tetramer. Two heparin-binding sites were observed on the surface and were present at the interface of each of the two beta-sheet dimers. The structure supports the formation of higher order oligomers of IP-10, as observed in recent in vivo studies with mouse IP-10, which will have functional relevance. Structure of mouse IP-10, a chemokine.,Jabeen T, Leonard P, Jamaluddin H, Acharya KR Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):611-9. Epub 2008, May 14. PMID:18560148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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