1mqt: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mqt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Swine_vesicular_disease_virus Swine vesicular disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mqt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Swine_vesicular_disease_virus Swine vesicular disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPL:OCTANOIC+ACID+(2-HYDROXY-1-HYDROXYMETHYL-HEPTADEC-3-ENYL)-AMIDE'>SPL</scene></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]] 3.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cov|1cov]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPL:OCTANOIC+ACID+(2-HYDROXY-1-HYDROXYMETHYL-HEPTADEC-3-ENYL)-AMIDE'>SPL</scene></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=1mqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqt OCA], [https://pdbe.org/1mqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqt RCSB], [https://www.ebi.ac.uk/pdbsum/1mqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqt ProSAT]</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=1mqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqt OCA], [https://pdbe.org/1mqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqt RCSB], [https://www.ebi.ac.uk/pdbsum/1mqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8B8X4_9ENTO Q8B8X4_9ENTO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mqt 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=1mqt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of swine vesicular disease virus (SVDV) was solved and refined at a 3.0-A resolution by X-ray crystallography to gain information about the role of sequence changes that occurred as this virus evolved from the parental human pathogen coxsackievirus B5 (CVB5). These amino acid substitutions can be clustered in five distinct regions: (i) the antigenic sites, (ii) the hydrophobic pocket of the VP1 beta-sandwich, (iii) the putative CAR binding site, (iv) the putative heparan sulfate binding site, and (v) the fivefold axis. The VP1 pocket is occupied by a branched pocket factor, apparently different from that present in the closely related virus CVB3 and in other picornaviruses. This finding may be relevant for the design of new antiviral compounds against this site. Density consistent with the presence of ions was observed on the fivefold and threefold axes. The structure also provided an accurate description of the putative receptor binding sites.
Structure of swine vesicular disease virus: mapping of changes occurring during adaptation of human coxsackie B5 virus to infect swine.,Verdaguer N, Jimenez-Clavero MA, Fita I, Ley V J Virol. 2003 Sep;77(18):9780-9. PMID:12941886<ref>PMID:12941886</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mqt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Swine vesicular disease virus]]
[[Category: Swine vesicular disease virus]]
[[Category: Fita, I]]
[[Category: Fita I]]
[[Category: Jimenez-Clavero, M A]]
[[Category: Jimenez-Clavero MA]]
[[Category: Ley, V]]
[[Category: Ley V]]
[[Category: Verdaguer, N]]
[[Category: Verdaguer N]]
[[Category: Enterovirus]]
[[Category: Icosahedral virus]]
[[Category: Svdv coat protein]]
[[Category: Virus]]

Latest revision as of 07:47, 14 February 2024

Swine Vesicular Disease Virus coat protein

1mqt, resolution 3.30Å

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