4GIZ
Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with LXXLL peptide of ubiquitin ligase E6AP at 2.55 A resolution
Summary for 4GIZ
| Entry DOI | 10.2210/pdb4giz/pdb |
| Related PRD ID | PRD_900035 |
| Descriptor | Maltose-binding periplasmic protein, UBIQUITIN LIGASE EA6P: chimeric protein, Protein E6, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | viral protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 119858.95 |
| Authors | McEwen, A.G.,Zanier, K.,Charbonnier, S.,Poussin, P.,Cura, V.,Vande Pol, S.,Trave, G.,Cavarelli, J. (deposition date: 2012-08-09, release date: 2013-01-23, Last modification date: 2024-02-28) |
| Primary citation | Zanier, K.,Charbonnier, S.,Sidi, A.O.,McEwen, A.G.,Ferrario, M.G.,Poussin-Courmontagne, P.,Cura, V.,Brimer, N.,Babah, K.O.,Ansari, T.,Muller, I.,Stote, R.H.,Cavarelli, J.,Vande Pol, S.,Trave, G. Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins. Science, 339:694-698, 2013 Cited by PubMed Abstract: 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. PubMed: 23393263DOI: 10.1126/science.1229934 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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