9FJ3

Structure of ubiquitin bound of coiled-coil UIM form 2

これはPDB形式変換不可エントリーです。

9FJ3 の概要

• エントリーDOI: 10.2210/pdb9fj3/pdb
• 分子名称: Polyubiquitin-C, GLU-GLN-GLU-ILE-GLU-GLU-LEU-GLU-ILE-GLU-ILE-ALA-ILE-LEU-LEU-SER-GLU-ILE-GLU-GLY, LYS-GLN-LYS-ILE-ALA-ALA-LEU-LYS-TYR-LYS-ILE-ALA-ALA-LEU-LYS-GLN-LYS-ILE, ... (5 entities in total)
• 機能のキーワード: ubiquitin, coiled-coil peptide, uim, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 27337.27

構造登録者

Paredes Vergara, P.,Huang, D.T. (登録日: 2024-05-30, 公開日: 2024-09-18, 最終更新日: 2024-10-16)

主引用文献

Vosbein, P.,Vergara, P.P.,Huang, D.T.,Thomson, A.R.
An engineered ubiquitin binding coiled coil peptide.
Chem Sci, 15:15776-15782, 2024

PubMed Abstract: Recognition of ubiquitin (Ub) is often mediated by small Ub binding domains such as the Ubiquitin Interacting Motif (UIM). Most Ub binding events are low affinity interactions, and designing stronger binders for Ub can be challenging. We here report the design of a short crosslinked coiled coil (CC) which is conformationally and chemically stable, and which can act as a scaffold to present the key binding residues from known UIM sequences. Doing so gives rise to a hybrid CC peptide that reconciles the important features of both UIM and CC sequences. We show by fluorescence polarization assays that this crosslinked 'CC-UIM' peptide exhibits enhanced binding to Ub compared to the original UIM sequence. Furthermore, we report a crystal structure of this peptide in complex with Ub. These studies show that preorganization of a small number of important binding residues onto a stable helical scaffold can be a successful strategy for binder design.

PubMed: 39268210
DOI: 10.1039/d4sc04204b

実験手法

X-RAY DIFFRACTION (1.4 Å)