8ep2
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ep2]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Aleutian_mink_disease_virus Aleutian mink disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ep2]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Aleutian_mink_disease_virus Aleutian mink disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EP2 FirstGlance]. <br> | ||
| - | </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=8ep2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ep2 OCA], [https://pdbe.org/8ep2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ep2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ep2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ep2 ProSAT]</span></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]] 2.37Å</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=8ep2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ep2 OCA], [https://pdbe.org/8ep2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ep2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ep2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ep2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CAPSD_ADVG CAPSD_ADVG] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 25 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 (10% abundance) and VP2 (90% abundance), which differ by the presence of an N-terminal extension in the minor protein VP1. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. VP1 binds DNA and may therefore play a role in viral DNA encapsidation.<ref>PMID:11602751</ref> <ref>PMID:2842956</ref> <ref>PMID:8380073</ref> | [https://www.uniprot.org/uniprot/CAPSD_ADVG CAPSD_ADVG] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 25 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 (10% abundance) and VP2 (90% abundance), which differ by the presence of an N-terminal extension in the minor protein VP1. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. VP1 binds DNA and may therefore play a role in viral DNA encapsidation.<ref>PMID:11602751</ref> <ref>PMID:2842956</ref> <ref>PMID:8380073</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Parvoviruses are small, single-stranded DNA viruses with non-enveloped capsids. Determining the capsid structures provides a framework for annotating regions important to the viral life cycle. Aleutian mink disease virus (AMDV), a pathogen in minks, and human parvovirus 4 (PARV4), infecting humans, are parvoviruses belonging to the genera Amdoparvovirus and Tetraparvovirus, respectively. While Aleutian mink disease caused by AMDV is a major threat to mink farming, no clear clinical manifestations have been established following infection with PARV4 in humans. Here, the capsid structures of AMDV and PARV4 were determined via cryo-electron microscopy at 2.37 and 3.12 A resolutions, respectively. Despite low amino acid sequence identities (10-30%) both viruses share the icosahedral nature of parvovirus capsids, with 60 viral proteins (VPs) assembling the capsid via two-, three-, and five-fold symmetry VP-related interactions, but display major structural variabilities in the surface loops when the capsid structures are superposed onto other parvoviruses. The capsid structures of AMDV and PARV4 will add to current knowledge of the structural platform for parvoviruses and permit future functional annotation of these viruses, which will help in understanding their infection mechanisms at a molecular level for the development of diagnostics and therapeutics. | ||
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| - | Capsid Structure of Aleutian Mink Disease Virus and Human Parvovirus 4: New Faces in the Parvovirus Family Portrait.,Lakshmanan R, Mietzsch M, Jimenez Ybargollin A, Chipman P, Fu X, Qiu J, Soderlund-Venermo M, McKenna R Viruses. 2022 Oct 9;14(10). pii: v14102219. doi: 10.3390/v14102219. PMID:36298773<ref>PMID:36298773</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 8ep2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
The capsid structure of Aleutian Mink Disease Virus
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