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| - | | + | #REDIRECT [[5w1o]] This PDB entry is obsolete and replaced by 5w1o |
| - | ==Crystal structure of HPV16 L1 Pentamer bound to Heparin oligosaccharides==
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| - | <StructureSection load='3oae' size='340' side='right' caption='[[3oae]], [[Resolution|resolution]] 2.80Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[3oae]] is a 5 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=3OAE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OAE FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r5h|2r5h]]</td></tr>
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| - | <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=3oae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oae OCA], [http://pdbe.org/3oae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oae RCSB], [http://www.ebi.ac.uk/pdbsum/3oae PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oae ProSAT]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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<ref>PMID:21115492</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3oae" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Human papilloma virus]]
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| - | [[Category: Chen, X S]]
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| - | [[Category: Dasgupta, J]]
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| - | [[Category: Capsid protein]]
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| - | [[Category: Jelly roll]]
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| - | [[Category: Receptor hspg]]
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| - | [[Category: Viral protein]]
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| - | [[Category: Virus capsid]]
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