2MXP

Solution structure of NDP52 ubiquitin-binding zinc finger

2MXP の概要

• エントリーDOI: 10.2210/pdb2mxp/pdb
• 関連するPDBエントリー: 4XKL
• NMR情報: BMRB: 25423
• 分子名称: Calcium-binding and coiled-coil domain-containing protein 2, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, ndp52, ubiquitin-binding, c2h2-type, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, perinuclear region : Q13137
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3952.95

構造登録者

Pan, L.,Xie, X. (登録日: 2015-01-12, 公開日: 2015-11-11, 最終更新日: 2024-05-15)

主引用文献

Xie, X.,Li, F.,Wang, Y.,Wang, Y.,Lin, Z.,Cheng, X.,Liu, J.,Chen, C.,Pan, L.
Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2
Autophagy, 11:1775-1789, 2015

PubMed Abstract: The autophagy receptor CALCOCO2/NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invading pathogens by specifically recognizing ubiquitin-coated intracellular pathogens and subsequently targeting them to the autophagic machinery; thereby it is required for innate immune defense against a range of infectious pathogens in mammals. However, the mechanistic basis underlying CALCOCO2-mediated specific recognition of ubiqutinated pathogens is still unknown. Here, using biochemical and structural analyses, we demonstrated that the cargo-binding region of CALCOCO2 contains a dynamic unconventional zinc finger as well as a C2H2-type zinc-finger, and only the C2H2-type zinc finger specifically recognizes mono-ubiquitin or poly-ubiquitin chains. In addition to elucidating the specific ubiquitin recognition mechanism of CALCOCO2, the structure of the CALCOCO2 C2H2-type zinc finger in complex with mono-ubiquitin also uncovers a unique zinc finger-binding mode for ubiquitin. Our findings provide mechanistic insight into how CALCOCO2 targets ubiquitin-decorated pathogens for autophagic degradations.

PubMed: 26506893
DOI: 10.1080/15548627.2015.1082025

実験手法

SOLUTION NMR