3ofl
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of Humanpapillomavirus18 (HPV18) capsid L1 pentamers bound to heparin oligosaccharides== | |
| - | + | <StructureSection load='3ofl' size='340' side='right' caption='[[3ofl]], [[Resolution|resolution]] 3.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ofl]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_18 Human papillomavirus type 18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OFL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JHM:2-DEOXY-6-O-SULFO-ALPHA-D-ARABINO-HEXOPYRANOSE'>JHM</scene>, <scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r5i|2r5i]]</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 Human papillomavirus type 18])</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=3ofl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofl RCSB], [http://www.ebi.ac.uk/pdbsum/3ofl PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21115492</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Human papillomavirus type 18]] | [[Category: Human papillomavirus type 18]] | ||
| - | [[Category: Chen, X S | + | [[Category: Chen, X S]] |
| - | [[Category: Dasgupta, J | + | [[Category: Dasgupta, J]] |
[[Category: Binds to host receptor]] | [[Category: Binds to host receptor]] | ||
[[Category: Capsid protein]] | [[Category: Capsid protein]] | ||
Revision as of 07:09, 19 December 2014
Crystal structure of Humanpapillomavirus18 (HPV18) capsid L1 pentamers bound to heparin oligosaccharides
| |||||||||||
