1EQX

SOLUTION STRUCTURE DETERMINATION AND MUTATIONAL ANALYSIS OF THE PAPILLOMAVIRUS E6-INTERACTING PEPTIDE OF E6AP

1EQX の概要

• エントリーDOI: 10.2210/pdb1eqx/pdb
• NMR情報: BMRB: 4607
• 分子名称: PAPILLOMAVIRUS E6-ASSOCIATED PROTEIN (1 entity in total)
• 機能のキーワード: alpha helix, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (Probable): Q05086
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2101.32

構造登録者

Be, X.,Hong, Y.,Androphy, E.J.,Chen, J.J.,Baleja, J.D. (登録日: 2000-04-06, 公開日: 2001-02-28, 最終更新日: 2024-05-22)

主引用文献

Be, X.,Hong, Y.,Wei, J.,Androphy, E.J.,Chen, J.J.,Baleja, J.D.
Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP.
Biochemistry, 40:1293-1299, 2001

PubMed Abstract: E6AP is a cellular protein that binds cancer-related papillomaviral E6 proteins. The E6 binding domain, called E6ap, is located on an 18-amino acid segment of E6AP. The corresponding peptide was synthesized and its structure determined by nuclear magnetic resonance spectroscopy. The overall structure of the peptide is helical. A consensus E6-binding sequence among different E6 interacting proteins contains three conserved hydrophobic residues. In the structure of the E6AP peptide, the three conserved leucines (Leu 9, Leu 12, and Leu 13) form a hydrophobic patch on one face of the alpha-helix. Substitution of any of these leucines with alanine abolished binding to E6 protein, indicating that the entire hydrophobic patch is necessary. Mutation of a glutamate to proline, but not alanine, also disrupted the interaction between E6 and E6AP protein, suggesting that the E6-binding motif of the E6AP protein must be helical when bound to E6. Comparison of the E6ap structure and mutational results with those of another E6-binding protein (E6BP/ERC-55) indicates the existence of a general E6-binding motif.

PubMed: 11170455
DOI: 10.1021/bi0019592

実験手法

SOLUTION NMR