3k7b

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[[Image:3k7b.png|left|200px]]
 
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==The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.==
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The line below this paragraph, containing "STRUCTURE_3k7b", creates the "Structure Box" on the page.
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<StructureSection load='3k7b' size='340' side='right'caption='[[3k7b]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3k7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_WR Vaccinia virus WR]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K7B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3k7b| PDB=3k7b | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7b OCA], [https://pdbe.org/3k7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k7b RCSB], [https://www.ebi.ac.uk/pdbsum/3k7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PG161_VACCW PG161_VACCW] Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails (PubMed:11119600, PubMed:23255618, PubMed:31941777). Therefore plays an essential role in efficient cell-to-cell spread of viral particles.<ref>PMID:11119600</ref> <ref>PMID:14581563</ref> <ref>PMID:23255618</ref> <ref>PMID:31941777</ref> <ref>PMID:9557708</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/3k7b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3k7b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions of N-linked glycosylations and the epitope of a protective antibody.
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===The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.===
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The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.,Su HP, Singh K, Gittis AG, Garboczi DN J Virol. 2010 Mar;84(5):2502-10. Epub 2009 Dec 23. PMID:20032175<ref>PMID:20032175</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_20032175}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3k7b" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20032175 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20032175}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3k7b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus_wr Vaccinia virus wr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7B OCA].
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[[Category: Vaccinia virus WR]]
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[[Category: Garboczi DN]]
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==Reference==
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[[Category: Su HP]]
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<ref group="xtra">PMID:020032175</ref><references group="xtra"/>
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[[Category: Vaccinia virus wr]]
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[[Category: Garboczi, D N.]]
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[[Category: Su, H P.]]
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[[Category: C-type lectin-like domain]]
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[[Category: Eev]]
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[[Category: Ev]]
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[[Category: Homodimer]]
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[[Category: Poxvirus]]
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[[Category: Viral protein]]
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Current revision

The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.

PDB ID 3k7b

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