3PY7

Crystal structure of full-length Bovine Papillomavirus oncoprotein E6 in complex with LD1 motif of paxillin at 2.3A resolution

Summary for 3PY7

• Entry DOI: 10.2210/pdb3py7/pdb
• Related PRD ID: PRD_900009
• Descriptor: maltose-binding periplasmic protein,paxillin LD1,protein E6 chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• Functional Keywords: viral protein
• Biological source: Escherichia coli; More
• Cellular location: Host cytoplasm : P06931
• Total number of polymer chains: 1
• Total formula weight: 58389.07

Authors

Cavarelli, J. (deposition date: 2010-12-12, release date: 2011-12-14, Last modification date: 2024-02-21)

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

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: 23393263
DOI: 10.1126/science.1229934

Experimental method

X-RAY DIFFRACTION (2.288 Å)