3BCZ

Crystal structure of Memo

3BCZ の概要

• エントリーDOI: 10.2210/pdb3bcz/pdb
• 関連するPDBエントリー: 3BD0
• 分子名称: Protein MEMO1, GLYCEROL (3 entities in total)
• 機能のキーワード: alpha/beta structure, peptide binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 135099.41

構造登録者

Qiu, C. (登録日: 2007-11-13, 公開日: 2007-11-27, 最終更新日: 2024-11-06)

主引用文献

Qiu, C.,Lienhard, S.,Hynes, N.E.,Badache, A.,Leahy, D.J.
Memo Is Homologous to Nonheme Iron Dioxygenases and Binds an ErbB2-derived Phosphopeptide in Its Vestigial Active Site.
J.Biol.Chem., 283:2734-2740, 2008

PubMed Abstract: Memo (mediator of ErbB2-driven cell motility) is a 297-amino-acid protein recently shown to co-precipitate with the C terminus of ErbB2 and be required for ErbB2-driven cell motility. Memo is not homologous to any known signaling proteins, and how it mediates ErbB2 signals is not known. To provide a molecular basis for understanding Memo function, we have determined and report here the 2.1A crystal structure of human Memo and show it be homologous to class III nonheme iron-dependent dioxygenases, a structural class that now includes a zinc-binding protein of unknown function. No metal binding or enzymatic activity can be detected for Memo, but Memo does bind directly to a specific ErbB2-derived phosphopeptide encompassing Tyr-1227 using its vestigial enzymatic active site. Memo thus represents a new class of phosphotyrosine-binding protein.

PubMed: 18045866
DOI: 10.1074/jbc.M703523200

実験手法

X-RAY DIFFRACTION (2.1 Å)