5jb1

From Proteopedia

(Difference between revisions)

Revision as of 11:27, 23 March 2022

Pseudo-atomic structure of Human Papillomavirus Type 59 L1 Virus-like Particle

5jb1, resolution 6.00Å

Structural highlights

5jb1 is a 6 chain structure with sequence from Hpv59. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5j6r
Gene:	ORF putative L1, L1 (HPV59)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q81971_HPV59] Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2.[RuleBase:RU361248][SAAS:SAAS00505820]

Publication Abstract from PubMed

Cervical cancer is the second most prevalent malignant tumor among women worldwide. High-risk human papillomaviruses (HPVs) are believed to be the major causative pathogens of mucosal epithelial cancers including cervical cancer. The HPV capsid is made up of 360 copies of major (L1) and 72 copies of minor (L2) capsid proteins. To date, limited high-resolution structural information about the HPV capsid has hindered attempts to understand details concerning the mechanisms by which HPV assembles and infects cells. In this study, we have constructed a pseudo-atomic model of the HPV59 L1-only capsid and demonstrate that the C-terminal arm of L1 participates in virus-host interactions. Moreover, when conjugated to a scaffold protein, keyhole limpet hemocyanin (KLH), this arm is immunogenic in vivo. These results provide new insights that will help elucidate HPV biology, and hence pave a way for the design of next-generation HPV vaccines.

The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction.,Li Z, Yan X, Yu H, Wang D, Song S, Li Y, He M, Hong Q, Zheng Q, Zhao Q, Gu Y, Zhang J, Janssen ME, Cardone G, Olson NH, Baker TS, Li S, Xia N Structure. 2016 Jun 7;24(6):874-85. doi: 10.1016/j.str.2016.04.008. PMID:27276427^[1]

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

References

↑ Li Z, Yan X, Yu H, Wang D, Song S, Li Y, He M, Hong Q, Zheng Q, Zhao Q, Gu Y, Zhang J, Janssen ME, Cardone G, Olson NH, Baker TS, Li S, Xia N. The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction. Structure. 2016 Jun 7;24(6):874-85. doi: 10.1016/j.str.2016.04.008. PMID:27276427 doi:http://dx.doi.org/10.1016/j.str.2016.04.008

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jb1"

@@ Line 3: / Line 3: @@
 <SX load='5jb1' size='340' side='right' viewer='molstar' caption='[[5jb1]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jb1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Hpv59 Hpv59]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JB1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JB1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jb1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hpv59 Hpv59]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JB1 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j6r|5j6r]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5j6r|5j6r]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF putative L1, L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37115 HPV59])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF putative L1, L1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37115 HPV59])</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=5jb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jb1 OCA], [http://pdbe.org/5jb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jb1 RCSB], [http://www.ebi.ac.uk/pdbsum/5jb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jb1 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=5jb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jb1 OCA], [https://pdbe.org/5jb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jb1 RCSB], [https://www.ebi.ac.uk/pdbsum/5jb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jb1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q81971_HPV59 Q81971_HPV59]] Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2.[RuleBase:RU361248][SAAS:SAAS00505820]
+[[https://www.uniprot.org/uniprot/Q81971_HPV59 Q81971_HPV59]] Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2.[RuleBase:RU361248][SAAS:SAAS00505820]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Major capsid protein L1|Major capsid protein L1]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

5jb1

From Proteopedia

Revision as of 11:27, 23 March 2022

Pseudo-atomic structure of Human Papillomavirus Type 59 L1 Virus-like Particle

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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