2uwi: Difference between revisions
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< | ==Structure of CrmE, a poxvirus TNF receptor== | ||
<StructureSection load='2uwi' size='340' side='right'caption='[[2uwi]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2uwi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Lister Vaccinia virus Lister]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UWI 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]] 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=2uwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwi OCA], [https://pdbe.org/2uwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwi RCSB], [https://www.ebi.ac.uk/pdbsum/2uwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwi ProSAT]</span></td></tr> | ||
</table> | |||
== 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/uw/2uwi_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=2uwi ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vaccinia virus (VACV), the smallpox vaccine, encodes many proteins that subvert the host immune response. One of these, cytokine response modifier E (CrmE), is secreted by infected cells and protects these cells from apoptotic challenge by tumour necrosis factor alpha (TNFalpha). We have expressed recombinant CrmE from VACV strain Lister in Escherichia coli, shown that the purified protein is monomeric in solution and competent to bind TNFalpha, and solved the structure to 2.0 A resolution. This is the first structure of a virus-encoded tumour necrosis factor receptor (TNFR). CrmE shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75; TNFR type 2). The structure confirms that CrmE adopts the canonical TNFR fold but only one of the two "ligand-binding" loops of TNFRSF1A is conserved in CrmE, suggesting a mechanism for the higher affinity of poxvirus TNFRs for TNFalpha over lymphotoxin-alpha. The roles of dimerisation and pre-ligand-assembly domains (PLADs) in poxvirus and mammalian TNFR activity are discussed. | Vaccinia virus (VACV), the smallpox vaccine, encodes many proteins that subvert the host immune response. One of these, cytokine response modifier E (CrmE), is secreted by infected cells and protects these cells from apoptotic challenge by tumour necrosis factor alpha (TNFalpha). We have expressed recombinant CrmE from VACV strain Lister in Escherichia coli, shown that the purified protein is monomeric in solution and competent to bind TNFalpha, and solved the structure to 2.0 A resolution. This is the first structure of a virus-encoded tumour necrosis factor receptor (TNFR). CrmE shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75; TNFR type 2). The structure confirms that CrmE adopts the canonical TNFR fold but only one of the two "ligand-binding" loops of TNFRSF1A is conserved in CrmE, suggesting a mechanism for the higher affinity of poxvirus TNFRs for TNFalpha over lymphotoxin-alpha. The roles of dimerisation and pre-ligand-assembly domains (PLADs) in poxvirus and mammalian TNFR activity are discussed. | ||
Structure of CrmE, a virus-encoded tumour necrosis factor receptor.,Graham SC, Bahar MW, Abrescia NG, Smith GL, Stuart DI, Grimes JM J Mol Biol. 2007 Sep 21;372(3):660-71. Epub 2007 Jul 3. PMID:17681535<ref>PMID:17681535</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2uwi" style="background-color:#fffaf0;"></div> | ||
[[Category: Vaccinia virus]] | == References == | ||
[[Category: Abrescia | <references/> | ||
[[Category: Bahar | __TOC__ | ||
[[Category: Graham | </StructureSection> | ||
[[Category: Grimes | [[Category: Large Structures]] | ||
[[Category: Smith | [[Category: Vaccinia virus Lister]] | ||
[[Category: Stuart | [[Category: Abrescia NG]] | ||
[[Category: Bahar MW]] | |||
[[Category: Graham SC]] | |||
[[Category: Grimes JM]] | |||
[[Category: Smith GL]] | |||
[[Category: Stuart DI]] | |||
Latest revision as of 01:25, 21 November 2024
Structure of CrmE, a poxvirus TNF receptor
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