3PY7

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

3PY7 の概要

• エントリーDOI: 10.2210/pdb3py7/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900009
• 分子名称: 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)
• 機能のキーワード: viral protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Host cytoplasm : P06931
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58389.07

構造登録者

Cavarelli, J. (登録日: 2010-12-12, 公開日: 2011-12-14, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.288 Å)