3py7
From Proteopedia
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- | [[ | + | ==Crystal structure of full-length Bovine Papillomavirus oncoprotein E6 in complex with LD1 motif of paxillin at 2.3A resolution== |
+ | <StructureSection load='3py7' size='340' side='right' caption='[[3py7]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3py7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PY7 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE,PXN,E6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10559 Bovine papillomavirus type 1])</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=3py7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3py7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3py7 RCSB], [http://www.ebi.ac.uk/pdbsum/3py7 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | E6 viral oncoproteins are key players in epithelial tumors induced by papillomaviruses in vertebrates, including cervical cancer in humans. E6 proteins target many host proteins by specifically interacting with acidic LxxLL motifs. We solved the crystal structures of bovine (BPV1) and human (HPV16) papillomavirus E6 proteins bound to LxxLL peptides from the focal adhesion protein paxillin and the ubiquitin ligase E6AP, respectively. In both E6 proteins, two zinc domains and a linker helix form a basic-hydrophobic pocket, which captures helical LxxLL motifs in a way compatible with other interaction modes. Mutational inactivation of the LxxLL binding pocket disrupts the oncogenic activities of both E6 proteins. This work reveals the structural basis of both the multifunctionality and the oncogenicity of E6 proteins. | ||
- | + | Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins.,Zanier K, Charbonnier S, Sidi AO, McEwen AG, Ferrario MG, Poussin-Courmontagne P, Cura V, Brimer N, Babah KO, Ansari T, Muller I, Stote RH, Cavarelli J, Vande Pol S, Trave G Science. 2013 Feb 8;339(6120):694-8. doi: 10.1126/science.1229934. PMID:23393263<ref>PMID:23393263</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Bovine papillomavirus type 1]] | [[Category: Bovine papillomavirus type 1]] | ||
- | [[Category: Cavarelli, J | + | [[Category: Cavarelli, J]] |
[[Category: Viral protein]] | [[Category: Viral protein]] |
Revision as of 11:49, 9 December 2014
Crystal structure of full-length Bovine Papillomavirus oncoprotein E6 in complex with LD1 motif of paxillin at 2.3A resolution
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