1o80: Difference between revisions
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<StructureSection load='1o80' size='340' side='right'caption='[[1o80]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1o80' size='340' side='right'caption='[[1o80]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1o80]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O80 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1o80]] is a 2 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=1O80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O80 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1o80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o80 OCA], [https://pdbe.org/1o80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o80 RCSB], [https://www.ebi.ac.uk/pdbsum/1o80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o80 ProSAT]</span></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=1o80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o80 OCA], [https://pdbe.org/1o80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o80 RCSB], [https://www.ebi.ac.uk/pdbsum/1o80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o80 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CXL10_HUMAN CXL10_HUMAN] Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Acharya | [[Category: Acharya KR]] | ||
[[Category: Holloway | [[Category: Holloway DE]] | ||
[[Category: Papageorgiou | [[Category: Papageorgiou AC]] | ||
[[Category: Swaminathan | [[Category: Swaminathan GJ]] | ||
Revision as of 15:30, 13 December 2023
Crystal structure of IP-10 H-FormCrystal structure of IP-10 H-Form
Structural highlights
FunctionCXL10_HUMAN Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3. 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 PubMedWe have determined the structure of wild-type IP-10 from three crystal forms. The crystals provide eight separate models of the IP-10 chain, all differing substantially from a monomeric IP-10 variant examined previously by NMR spectroscopy. In each crystal form, IP-10 chains form conventional beta sheet dimers, which, in turn, form a distinct tetrameric assembly. The M form tetramer is reminiscent of platelet factor 4, whereas the T and H forms feature a novel twelve-stranded beta sheet. Analytical ultracentrifugation indicates that, in free solution, IP-10 exists in a monomer-dimer equilibrium with a dissociation constant of 9 microM. We propose that the tetrameric structures may represent species promoted by the binding of glycosaminoglycans. The binding sites for several IP-10-neutralizing mAbs have also been mapped. Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine.,Swaminathan GJ, Holloway DE, Colvin RA, Campanella GK, Papageorgiou AC, Luster AD, Acharya KR Structure. 2003 May;11(5):521-32. PMID:12737818[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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