7KEO

Crystal structure of K29-linked di-ubiquitin in complex with synthetic antigen binding fragment

7KEO の概要

• エントリーDOI: 10.2210/pdb7keo/pdb
• 分子名称: Synthetic antigen binding fragment, heavy chain, Synthetic antigen binding fragment, light chain, Ubiquitin, ... (5 entities in total)
• 機能のキーワード: protein 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: 8
• 化学式量合計: 131636.67

構造登録者

Yu, Y.,Zheng, Q.,Erramilli, S.,Pan, M.,Kossiakoff, A.,Liu, L.,Zhao, M. (登録日: 2020-10-11, 公開日: 2021-07-28, 最終更新日: 2024-11-13)

主引用文献

Yu, Y.,Zheng, Q.,Erramilli, S.K.,Pan, M.,Park, S.,Xie, Y.,Li, J.,Fei, J.,Kossiakoff, A.A.,Liu, L.,Zhao, M.
K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle.
Nat.Chem.Biol., 17:896-905, 2021

PubMed Abstract: Protein ubiquitination shows remarkable topological and functional diversity through the polymerization of ubiquitin via different linkages. Deciphering the cellular ubiquitin code is of central importance to understand the physiology of the cell. However, our understanding of its function is rather limited due to the lack of specific binders as tools to detect K29-linked polyubiquitin. In this study, we screened and characterized a synthetic antigen-binding fragment, termed sAB-K29, that can specifically recognize K29-linked polyubiquitin using chemically synthesized K29-linked diubiquitin. We further determined the crystal structure of this fragment bound to the K29-linked diubiquitin, which revealed the molecular basis of specificity. Using sAB-K29 as a tool, we uncovered that K29-linked ubiquitination is involved in different kinds of cellular proteotoxic stress response as well as cell cycle regulation. In particular, we showed that K29-linked ubiquitination is enriched in the midbody and downregulation of the K29-linked ubiquitination signal arrests cells in G1/S phase.

PubMed: 34239127
DOI: 10.1038/s41589-021-00823-5

実験手法

X-RAY DIFFRACTION (2.9 Å)