3f62: Difference between revisions

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==Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein==
==Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein==
<StructureSection load='3f62' size='340' side='right' caption='[[3f62]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3f62' size='340' side='right'caption='[[3f62]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3f62]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ectromelia_virus Ectromelia virus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F62 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3f62]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ectromelia_virus Ectromelia virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F62 FirstGlance]. <br>
</td></tr><tr><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 Homo sapiens])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f62 RCSB], [http://www.ebi.ac.uk/pdbsum/3f62 PDBsum]</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=3f62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f62 OCA], [https://pdbe.org/3f62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f62 RCSB], [https://www.ebi.ac.uk/pdbsum/3f62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f62 ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q85319_9POXV Q85319_9POXV]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/3f62_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/3f62_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3f62 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3f62" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Interleukin|Interleukin]]
*[[Interleukin 3D structures|Interleukin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Ectromelia virus]]
[[Category: Ectromelia virus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Deng, J.]]
[[Category: Large Structures]]
[[Category: Krumm, B E.]]
[[Category: Deng J]]
[[Category: Li, Y.]]
[[Category: Krumm BE]]
[[Category: Beta trefoil]]
[[Category: Li Y]]
[[Category: Cytokine]]
[[Category: Il-18]]
[[Category: Immunoglobulin]]
[[Category: Secreted]]

Latest revision as of 04:47, 21 November 2024

Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding ProteinCrystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein

Structural highlights

3f62 is a 2 chain structure with sequence from Ectromelia virus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q85319_9POXV

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 PubMed

Human interleukin-18 (hIL-18) is a cytokine that plays an important role in inflammation and host defense against microbes. Its activity is regulated in vivo by a naturally occurring antagonist, the human IL-18-binding protein (IL-18BP). Functional homologs of human IL-18BP are encoded by all orthopoxviruses, including variola virus, the causative agent of smallpox. They contribute to virulence by suppressing IL-18-mediated immune responses. Here, we describe the 2.0-A resolution crystal structure of an orthopoxvirus IL-18BP, ectromelia virus IL-18BP (ectvIL-18BP), in complex with hIL-18. The hIL-18 structure in the complex shows significant conformational change at the binding interface compared with the structure of ligand-free hIL-18, indicating that the binding is mediated by an induced-fit mechanism. EctvIL-18BP adopts a canonical Ig fold and interacts via one edge of its beta-sandwich with 3 cavities on the hIL-18 surface through extensive hydrophobic and hydrogen bonding interactions. Most of the ectvIL-18BP residues that participate in these interactions are conserved in both human and viral homologs, explaining their functional equivalence despite limited sequence homology. EctvIL-18BP blocks a putative receptor-binding site on IL-18, thus preventing IL-18 from engaging its receptor. Our structure provides insights into how IL-18BPs modulate hIL-18 activity. The revealed binding interface provides the basis for rational design of inhibitors against orthopoxvirus IL-18BP (for treating orthopoxvirus infection) or hIL-18 (for treating certain inflammatory and autoimmune diseases).

Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein.,Krumm B, Meng X, Li Y, Xiang Y, Deng J Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20711-5. Epub 2008 Dec 22. PMID:19104048[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Krumm B, Meng X, Li Y, Xiang Y, Deng J. Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein. Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20711-5. Epub 2008 Dec 22. PMID:19104048 doi:0809086106

3f62, resolution 2.00Å

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OCA