6gsi: Difference between revisions

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<SX load='6gsi' size='340' side='right' viewer='molstar' caption='[[6gsi]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
<SX load='6gsi' size='340' side='right' viewer='molstar' caption='[[6gsi]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6gsi]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Cat Cat] and [http://en.wikipedia.org/wiki/Feline_calicivirus_strain_f9 Feline calicivirus strain f9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6GSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[6gsi]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_calicivirus_strain_F9 Feline calicivirus strain F9] and [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.75&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gsh|6gsh]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F11R, JAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9685 Cat])</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=6gsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsi OCA], [https://pdbe.org/6gsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gsi RCSB], [https://www.ebi.ac.uk/pdbsum/6gsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6gsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsi OCA], [http://pdbe.org/6gsi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gsi RCSB], [http://www.ebi.ac.uk/pdbsum/6gsi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CAPSD_FCVF9 CAPSD_FCVF9]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm. [[http://www.uniprot.org/uniprot/VP2_FCVF9 VP2_FCVF9]] Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). [[http://www.uniprot.org/uniprot/JAM1_FELCA JAM1_FELCA]] Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation.[UniProtKB:O88792][UniProtKB:Q9Y624]  (Microbial infection) May act as a cellular receptor for calicivirus.<ref>PMID:16611908</ref> <ref>PMID:17913818</ref>  (Microbial infection) In case of orthoreovirus infection, serves as receptor for the virus.<ref>PMID:11239401</ref> 
[https://www.uniprot.org/uniprot/CAPSD_FCVF9 CAPSD_FCVF9] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Cat]]
[[Category: Feline calicivirus strain F9]]
[[Category: Feline calicivirus strain f9]]
[[Category: Felis catus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bhella, D]]
[[Category: Bhella D]]
[[Category: Conley, M J]]
[[Category: Conley MJ]]
[[Category: Calicivirus]]
[[Category: Capsid]]
[[Category: Junctional-adhesion molecule some]]
[[Category: Portal]]
[[Category: Vesivirus]]
[[Category: Virus]]
[[Category: Vp1]]
[[Category: Vp2]]

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