|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5w1x' size='340' side='right'caption='[[5w1x]], [[Resolution|resolution]] 3.37Å' scene=''> | | <StructureSection load='5w1x' size='340' side='right'caption='[[5w1x]], [[Resolution|resolution]] 3.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w1x]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Hpv18 Hpv18]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ofl 3ofl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W1X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5W1X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w1x]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_papillomavirus_type_18 Human papillomavirus type 18]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ofl 3ofl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W1X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene></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]] 3.374Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=JHM:2-DEOXY-6-O-SULFO-ALPHA-D-ARABINO-HEXOPYRANOSE'>JHM</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=JHM:2-DEOXY-6-O-SULFO-ALPHA-D-ARABINO-HEXOPYRANOSE'>JHM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=333761 HPV18])</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=5w1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w1x OCA], [https://pdbe.org/5w1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w1x RCSB], [https://www.ebi.ac.uk/pdbsum/5w1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w1x 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=5w1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w1x OCA], [http://pdbe.org/5w1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w1x RCSB], [http://www.ebi.ac.uk/pdbsum/5w1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w1x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q5G244_HPV18 Q5G244_HPV18]] 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:SAAS00514925] | + | [https://www.uniprot.org/uniprot/VL1_HPV18 VL1_HPV18] 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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Major capsid protein L1|Major capsid protein L1]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hpv18]] | + | [[Category: Human papillomavirus type 18]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, X S]] | + | [[Category: Chen XS]] |
| - | [[Category: Dasgupta, J]] | + | [[Category: Dasgupta J]] |
| - | [[Category: Binds to host receptor]]
| + | |
| - | [[Category: Capsid protein]]
| + | |
| - | [[Category: Jelly roll]]
| + | |
| - | [[Category: Protein oligosaccharide complex]]
| + | |
| - | [[Category: Receptor heparin oligosaccharide]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virus capsid]]
| + | |
| Structural highlights
Function
VL1_HPV18 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]
Publication Abstract from PubMed
The high-risk human papillomavirus types 16 (HPV16) and 18 (HPV18) can cause cervical cancer. Efficient infection by HPV16 and 18 pseudovirions requires interactions ofparticles with cell surface receptor heparan sulfate oligosaccharide. To understand the virus-receptor interactions for HPV infection, we determined the crystal structures of HPV16 and 18 capsids bound to the oligosaccharide receptor fragment using oligomeric heparin. The HPV-heparin structures revealed multiple binding sites for the highly negatively charged oligosaccharide fragment on the capsid surface, which is different from previously reported virus-receptor interactions where a single type of binding pocket is present for a particular receptor. We performed structure-guided mutagenesis to generate mutant viruses, and the cell binding and infectivity assays demonstrated the functional role of viral residues involved in heparin binding. These results provide a basis for understanding virus-heparan sulfate receptor interactions critical for HPV infection, and for the potential development of inhibitors against HPV infection.
Structural basis of oligosaccharide receptor recognition by human Papillomavirus.,Dasgupta J, Bienkowska-Haba M, Ortega ME, Patel HD, Bodevin S, Spillmann D, Bishop B, Sapp M, Chen XS J Biol Chem. 2010 Nov 30. PMID:21115492[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dasgupta J, Bienkowska-Haba M, Ortega ME, Patel HD, Bodevin S, Spillmann D, Bishop B, Sapp M, Chen XS. Structural basis of oligosaccharide receptor recognition by human Papillomavirus. J Biol Chem. 2010 Nov 30. PMID:21115492 doi:10.1074/jbc.M110.160184
|
