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==Pentamer structure of Major Capsid Protein L1 of Human Papilloma Virus type 16==
==Pentamer structure of Major Capsid Protein L1 of Human Papilloma Virus type 16==
<StructureSection load='2r5h' size='340' side='right' caption='[[2r5h]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='2r5h' size='340' side='right'caption='[[2r5h]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2r5h]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_papilloma_virus Human papilloma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R5H FirstGlance]. <br>
<table><tr><td colspan='2'>[[2r5h]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_papillomavirus Human papillomavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R5H FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dzl|1dzl]], [[2r5i|2r5i]], [[2r5j|2r5j]], [[2r5k|2r5k]]</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]] 3.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5h OCA], [http://pdbe.org/2r5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r5h RCSB], [http://www.ebi.ac.uk/pdbsum/2r5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r5h 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=2r5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5h OCA], [https://pdbe.org/2r5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r5h RCSB], [https://www.ebi.ac.uk/pdbsum/2r5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r5h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1U9YFU1_9PAPI A0A1U9YFU1_9PAPI] 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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r5h_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r5h_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 17: Line 19:
</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=2r5h 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=2r5h ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human papillomaviruses (HPVs) are known etiologic agents of cervical cancer. Vaccines that contain virus-like particles (VLPs) made of L1 capsid protein from several high risk HPV types have proven to be effective against HPV infections. Raising high levels of neutralizing antibodies against each HPV type is believed to be the primary mechanism of protection, gained by vaccination. Antibodies elicited by a particular HPV type are highly specific to that particular HPV type and show little or no cross-reactivity between HPV types. With an intention to understand the interplay between the L1 structure of different HPV types and the type specificity of neutralizing antibodies, we have prepared the L1 pentamers of four different HPV types, HPV11, HPV16, HPV18, and HPV35. The pentamers only bind the type-specific neutralizing monoclonal antibodies (NmAbs) that are raised against the VLP of the corresponding HPV type, implying that the surface loop structures of the pentamers from each type are distinctive and functionally active as VLPs in terms of antibody binding. We have determined the crystal structures of all four L1 pentamers, and their comparisons revealed characteristic conformational differences of the surface loops that contain the known epitopes for the NmAbs. On the basis of these distinct surface loop structures, we have provided a molecular explanation for the type specificity of NmAbs against HPV infection.


Crystal structures of four types of human papillomavirus L1 capsid proteins: understanding the specificity of neutralizing monoclonal antibodies.,Bishop B, Dasgupta J, Klein M, Garcea RL, Christensen ND, Zhao R, Chen XS J Biol Chem. 2007 Oct 26;282(43):31803-11. Epub 2007 Sep 4. PMID:17804402<ref>PMID:17804402</ref>
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2r5h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human papilloma virus]]
[[Category: Human papillomavirus]]
[[Category: Bishop, B]]
[[Category: Large Structures]]
[[Category: Chen, X S]]
[[Category: Bishop B]]
[[Category: Dasgupta, J]]
[[Category: Chen XS]]
[[Category: Capsid]]
[[Category: Dasgupta J]]
[[Category: Capsid protein]]
[[Category: Pentamer]]
[[Category: Protein]]
[[Category: Type specific epitope]]
[[Category: Viral protein]]
[[Category: Virion]]

Latest revision as of 12:19, 21 February 2024

Pentamer structure of Major Capsid Protein L1 of Human Papilloma Virus type 16Pentamer structure of Major Capsid Protein L1 of Human Papilloma Virus type 16

Structural highlights

2r5h is a 15 chain structure with sequence from Human papillomavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A1U9YFU1_9PAPI 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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2r5h, resolution 3.70Å

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