1ypy: Difference between revisions
No edit summary |
No edit summary |
||
(5 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Crystal Structure of Vaccinia Virus L1 protein== | ==Crystal Structure of Vaccinia Virus L1 protein== | ||
<StructureSection load='1ypy' size='340' side='right' caption='[[1ypy]], [[Resolution|resolution]] 1.51Å' scene=''> | <StructureSection load='1ypy' size='340' side='right'caption='[[1ypy]], [[Resolution|resolution]] 1.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ypy]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ypy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YPY 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]] 1.51Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ypy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypy OCA], [https://pdbe.org/1ypy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ypy RCSB], [https://www.ebi.ac.uk/pdbsum/1ypy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ypy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PG095_VACCW PG095_VACCW] Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.<ref>PMID:34076488</ref> | ||
== 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/yp/1ypy_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yp/1ypy_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <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/ | </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=1ypy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Line 26: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ypy" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
[[Category: Allison | [[Category: Allison TJ]] | ||
[[Category: Fogg | [[Category: Fogg C]] | ||
[[Category: Garboczi | [[Category: Garboczi DN]] | ||
[[Category: Garman | [[Category: Garman SC]] | ||
[[Category: Moss | [[Category: Moss B]] | ||
[[Category: Su | [[Category: Su HP]] | ||
Latest revision as of 10:32, 9 October 2024
Crystal Structure of Vaccinia Virus L1 proteinCrystal Structure of Vaccinia Virus L1 protein
Structural highlights
FunctionPG095_VACCW Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.[1] 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 PubMedAlthough eradicated from nature more than two decades ago, the threat of smallpox has reemerged because of concerns over its use as a biological weapon. We present the structure of the poxvirus L1 protein, a molecule that is conserved throughout the poxvirus family and is nearly identical in vaccinia virus and in variola virus, which causes smallpox. L1 is a myristoylated envelope protein that is a potent target for neutralizing antibodies and an important component of current experimental vaccines. The L1 structure reveals a hydrophobic cavity located adjacent to its N terminus. The cavity would be capable of shielding the myristate moiety, which is essential for virion assembly. The structure of L1 is a step in the elucidation of molecular mechanisms common to all poxviruses that may stimulate the design of safer vaccines and new antipoxvirus drugs. The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies.,Su HP, Garman SC, Allison TJ, Fogg C, Moss B, Garboczi DN Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4240-5. Epub 2005 Mar 10. PMID:15761054[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|