4pb6: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 4pb6~~ is ~~ON HOLD until sometime~~ in the ~~future~~

==Feline calicivirus VP1 T=1 virus-like particle==

== Structural highlights ==

<table><tr><td colspan='2'>[[4pb6]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_calicivirus Feline calicivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PB6 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]] 8Å</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=4pb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pb6 OCA], [https://pdbe.org/4pb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pb6 RCSB], [https://www.ebi.ac.uk/pdbsum/4pb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pb6 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A0A0J9X1Z3_9CALI A0A0J9X1Z3_9CALI]

== Publication Abstract from PubMed ==

The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahedral T=3 shell formed by the viral VP1 protein. Upon its expression in the insect cell - baculovirus system in the context of vaccine development, two types of virus-like particles (VLPs) were formed, a majority built of 60 subunits (T=1) and a minority probably built of 180 subunits (T=3). The structure of the small particles was determined by x-ray crystallography at 0.8 nm resolution helped by cryo-electron microscopy in order to understand their formation. Cubic crystals belonged to space group P213. Their self-rotation function showed the presence of an octahedral pseudo-symmetry similar to the one described previously by Agerbandje and co-workers for human parvovirus VLPs. The crystal structure could be solved starting from the published VP1 structure in the context of the T=3 viral capsid. In contrast to viral capsids, where the capsomers are interlocked by the exchange of the N-terminal arm (NTA) domain, this domain is disordered in the T=1 capsid of the VLPs. Furthermore it is prone to proteolytic cleavage. The relative orientation of P (protrusion) and S (shell) domains is alerted so as to fit VP1 to the smaller T=1 particle whereas the intermolecular contacts around 2-fold, 3-fold and 5-fold axes are conserved. By consequence the surface of the VLP is very similar compared to the viral capsid and suggests a similar antigenicity. The knowledge of the structure of the VLPs will help to improve their stability, in respect to a use for vaccination.

~~Authors:~~ Burmeister, W.P., ~~Buisson, M~~.

Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement.,Burmeister WP, Buisson M, Estrozi LF, Schoehn G, Billet O, Hannas Z, Sigoillot C, Poulet H PLoS One. 2015 Mar 20;10(3):e0119289. doi: 10.1371/journal.pone.0119289., eCollection 2015. PMID:25794153<ref>PMID:25794153</ref>

~~Description~~: Feline calicivirus ~~VP1 T=1 virus-like particle~~

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

</div>

==See Also==

*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Feline calicivirus]]

[[Category: Large Structures]]

[[Category: Buisson M]]

[[Category: Burmeister WP]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4pb6 is ON HOLD  until sometime in the future
+==Feline calicivirus VP1 T=1 virus-like particle==
+<StructureSection load='4pb6' size='340' side='right'caption='[[4pb6]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pb6]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_calicivirus Feline calicivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PB6 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]] 8&#8491;</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=4pb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pb6 OCA], [https://pdbe.org/4pb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pb6 RCSB], [https://www.ebi.ac.uk/pdbsum/4pb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pb6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0J9X1Z3_9CALI A0A0J9X1Z3_9CALI]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahedral T=3 shell formed by the viral VP1 protein. Upon its expression in the insect cell - baculovirus system in the context of vaccine development, two types of virus-like particles (VLPs) were formed, a majority built of 60 subunits (T=1) and a minority probably built of 180 subunits (T=3). The structure of the small particles was determined by x-ray crystallography at 0.8 nm resolution helped by cryo-electron microscopy in order to understand their formation. Cubic crystals belonged to space group P213. Their self-rotation function showed the presence of an octahedral pseudo-symmetry similar to the one described previously by Agerbandje and co-workers for human parvovirus VLPs. The crystal structure could be solved starting from the published VP1 structure in the context of the T=3 viral capsid. In contrast to viral capsids, where the capsomers are interlocked by the exchange of the N-terminal arm (NTA) domain, this domain is disordered in the T=1 capsid of the VLPs. Furthermore it is prone to proteolytic cleavage. The relative orientation of P (protrusion) and S (shell) domains is alerted so as to fit VP1 to the smaller T=1 particle whereas the intermolecular contacts around 2-fold, 3-fold and 5-fold axes are conserved. By consequence the surface of the VLP is very similar compared to the viral capsid and suggests a similar antigenicity. The knowledge of the structure of the VLPs will help to improve their stability, in respect to a use for vaccination.
-Authors: Burmeister, W.P., Buisson, M.
+Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement.,Burmeister WP, Buisson M, Estrozi LF, Schoehn G, Billet O, Hannas Z, Sigoillot C, Poulet H PLoS One. 2015 Mar 20;10(3):e0119289. doi: 10.1371/journal.pone.0119289., eCollection 2015. PMID:25794153<ref>PMID:25794153</ref>
-Description: Feline calicivirus VP1 T=1 virus-like particle
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4pb6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Feline calicivirus]]
+[[Category: Large Structures]]
+[[Category: Buisson M]]
+[[Category: Burmeister WP]]