1dzl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dzl' size='340' side='right'caption='[[1dzl]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1dzl' size='340' side='right'caption='[[1dzl]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_papillomavirus_type_16 Human papillomavirus type 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZL 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=1dzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzl OCA], [https://pdbe.org/1dzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzl RCSB], [https://www.ebi.ac.uk/pdbsum/1dzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzl ProSAT]</span></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]] 3.5Å</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=1dzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzl OCA], [https://pdbe.org/1dzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzl RCSB], [https://www.ebi.ac.uk/pdbsum/1dzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VL1_HPV16 VL1_HPV16] 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.[HAMAP-Rule:MF_04002]<ref>PMID:12610160</ref> <ref>PMID:26289843</ref> <ref>PMID:8553535</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1dzl 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=1dzl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The papillomavirus major late protein, L1, forms the pentameric assembly unit of the viral shell. Recombinant HPV16 L1 pentamers assemble in vitro into capsid-like structures, and truncation of ten N-terminal residues leads to a homogeneous preparation of 12-pentamer, icosahedral particles. X-ray crystallographic analysis of these particles at 3.5 A resolution shows that L1 closely resembles VP1 from polyomaviruses. Surface loops contain the sites of sequence variation among HPV types and the locations of dominant neutralizing epitopes. The ease with which small virus-like particles may be obtained from L1 expressed in E. coli makes them attractive candidate components of a papillomavirus vaccine. Their crystal structure also provides a starting point for future vaccine design. | ||
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| - | Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16.,Chen XS, Garcea RL, Goldberg I, Casini G, Harrison SC Mol Cell. 2000 Mar;5(3):557-67. PMID:10882140<ref>PMID:10882140</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dzl" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human papillomavirus type 16]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chen | + | [[Category: Chen XJ]] |
| - | [[Category: Garcea | + | [[Category: Garcea B]] |
| - | [[Category: Goldberge | + | [[Category: Goldberge I]] |
| - | [[Category: Harrison | + | [[Category: Harrison SC]] |
| - | + | ||
| - | + | ||
Revision as of 09:56, 20 March 2024
L1 protein of human papillomavirus 16
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