2C7N

Human Rabex-5 residues 1-74 in complex with Ubiquitin

2C7N の概要

• エントリーDOI: 10.2210/pdb2c7n/pdb
• 関連するPDBエントリー: 1AAR 1E0Q 1P3Q 1UZX 1V80 1V81 1WR6 1WRD 1YD8 2BGF 2C7M
• 分子名称: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1, UBIQUITIN, ZINC ION, ... (4 entities in total)
• 機能のキーワード: protein-binding, ubiquitin binding domain, endocytosis, nuclear protein, polyprotein, ubiquitin complex, protein binding
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 104562.01

構造登録者

Penengo, L.,Mapelli, M.,Murachelli, A.G.,Confalioneri, S.,Magri, L.,Musacchio, A.,Di Fiore, P.P.,Polo, S.,Schneider, T.R. (登録日: 2005-11-25, 公開日: 2006-02-15, 最終更新日: 2024-05-08)

主引用文献

Penengo, L.,Mapelli, M.,Murachelli, A.G.,Confalonieri, S.,Magri, L.,Musacchio, A.,Di Fiore, P.P.,Polo, S.,Schneider, T.R.
Crystal Structure of the Ubiquitin Binding Domains of Rabex-5 Reveals Two Modes of Interaction with Ubiquitin.
Cell(Cambridge,Mass.), 124:1183-, 2006

PubMed Abstract: The interaction between ubiquitinated proteins and intracellular proteins harboring ubiquitin binding domains (UBDs) is critical to a multitude of cellular processes. Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to Ub through two independent UBDs. These UBDs determine a number of properties of Rabex-5, including its coupled monoubiquitination and interaction in vivo with ubiquitinated EGFRs. Structural and biochemical characterization of the UBDs of Rabex-5 revealed that one of them (MIU, motif interacting with ubiquitin) binds to Ub with modes superimposable to those of the UIM (ubiquitin-interacting motif):Ub interaction, although in the opposite orientation. The other UBD, RUZ (Rabex-5 ubiquitin binding zinc finger) binds to a surface of Ub centered on Asp58(Ub) and distinct from the "canonical" Ile44(Ub)-based surface. The two binding surfaces allow Ub to interact simultaneously with different UBDs, thus opening new perspectives in Ub-mediated signaling.

PubMed: 16499958
DOI: 10.1016/J.CELL.2006.02.020

実験手法

X-RAY DIFFRACTION (2.1 Å)