|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4xfu' size='340' side='right'caption='[[4xfu]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='4xfu' size='340' side='right'caption='[[4xfu]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xfu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XFU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xfu]] 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=4XFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XFU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xfs|4xfs]], [[4xft|4xft]]</td></tr> | + | </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=4xfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfu OCA], [https://pdbe.org/4xfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xfu RCSB], [https://www.ebi.ac.uk/pdbsum/4xfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfu ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL18, IGIF, IL1F4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfu OCA], [http://pdbe.org/4xfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xfu RCSB], [http://www.ebi.ac.uk/pdbsum/4xfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN]] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. | + | [https://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 24: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deng, J]] | + | [[Category: Deng J]] |
| - | [[Category: Krumm, B E]] | + | [[Category: Krumm BE]] |
| - | [[Category: Meng, X]] | + | [[Category: Meng X]] |
| - | [[Category: Xiang, Y]] | + | [[Category: Xiang Y]] |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Il-18]]
| + | |
| - | [[Category: Immune defense]]
| + | |
| - | [[Category: Interleukin-18]]
| + | |
| - | [[Category: Surface entropy reduction]]
| + | |
| Structural highlights
Function
IL18_HUMAN Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.
Publication Abstract from PubMed
Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.
Crystallization of interleukin-18 for structure-based inhibitor design.,Krumm B, Meng X, Xiang Y, Deng J Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):710-7. doi:, 10.1107/S2053230X15006871. Epub 2015 May 20. PMID:26057800[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krumm B, Meng X, Xiang Y, Deng J. Crystallization of interleukin-18 for structure-based inhibitor design. Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):710-7. doi:, 10.1107/S2053230X15006871. Epub 2015 May 20. PMID:26057800 doi:http://dx.doi.org/10.1107/S2053230X15006871
|
