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2ljx
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ljx' size='340' side='right' caption='[[2ljx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2ljx' size='340' side='right' caption='[[2ljx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2ljx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus Human papillomavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LJX OCA]. <br> | + | <table><tr><td colspan='2'>[[2ljx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus Human papillomavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LJX OCA]. <br> |
| - | <b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> |
| - | <b>[[Related_structure|Related:]]</b> [[2ljy|2ljy]], [[2ljz|2ljz]]< | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ljy|2ljy]], [[2ljz|2ljz]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10566 Human papillomavirus])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ljx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ljx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ljx RCSB], [http://www.ebi.ac.uk/pdbsum/2ljx PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ljx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ljx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ljx RCSB], [http://www.ebi.ac.uk/pdbsum/2ljx PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The viral oncoprotein E6 is an essential factor for cervical cancers induced by "high-risk" mucosal HPV. Among other oncogenic activities, E6 recruits the ubiquitin ligase E6AP to promote the ubiquitination and subsequent proteasomal degradation of p53. E6 is prone to self-association, which long precluded its structural analysis. Here we found that E6 specifically dimerizes through its N-terminal domain and that disruption of the dimer interface strongly increases E6 solubility. This allowed us to raise structural data covering the entire HPV16 E6 protein, including the high-resolution NMR structures of the two zinc-binding domains of E6 and a robust data-driven model structure of the N-terminal domain homodimer. Interestingly, homodimer interface mutations that disrupt E6 self-association also inactivate E6-mediated p53 degradation. These data suggest that E6 needs to self-associate via its N-terminal domain to promote the polyubiquitination of p53 by E6AP. | The viral oncoprotein E6 is an essential factor for cervical cancers induced by "high-risk" mucosal HPV. Among other oncogenic activities, E6 recruits the ubiquitin ligase E6AP to promote the ubiquitination and subsequent proteasomal degradation of p53. E6 is prone to self-association, which long precluded its structural analysis. Here we found that E6 specifically dimerizes through its N-terminal domain and that disruption of the dimer interface strongly increases E6 solubility. This allowed us to raise structural data covering the entire HPV16 E6 protein, including the high-resolution NMR structures of the two zinc-binding domains of E6 and a robust data-driven model structure of the N-terminal domain homodimer. Interestingly, homodimer interface mutations that disrupt E6 self-association also inactivate E6-mediated p53 degradation. These data suggest that E6 needs to self-associate via its N-terminal domain to promote the polyubiquitination of p53 by E6AP. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:40, 1 May 2014
Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein
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