5Z7G

Crystal structure of TAX1BP1 SKICH region in complex with NAP1

5Z7G の概要

• エントリーDOI: 10.2210/pdb5z7g/pdb
• 関連するPDBエントリー: 5Z7A
• 分子名称: Tax1-binding protein 1, 5-azacytidine-induced protein 2, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: tax1bp1, nap1, skich domain, autophagy receptor, selective autophagy, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38669.77

構造登録者

Pan, L.F.,Fu, T.,Liu, J.P.,Xie, X.Q.,Wang, Y.L.,Hu, S.C. (登録日: 2018-01-28, 公開日: 2019-01-02, 最終更新日: 2023-11-22)

主引用文献

Fu, T.,Liu, J.,Wang, Y.,Xie, X.,Hu, S.,Pan, L.
Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1
Proc. Natl. Acad. Sci. U.S.A., 115:E11651-E11660, 2018

PubMed Abstract: NDP52 and TAX1BP1, two SKIP carboxyl homology (SKICH) domain-containing autophagy receptors, play crucial roles in selective autophagy. The autophagic functions of NDP52 and TAX1BP1 are regulated by TANK-binding kinase 1 (TBK1), which may associate with them through the adaptor NAP1. However, the molecular mechanism governing the interactions of NAP1 with NDP52 and TAX1BP1, as well as the effects induced by TBK1-mediated phosphorylation of NDP52 and TAX1BP1, remains elusive. Here, we report the atomic structures of the SKICH regions of NDP52 and TAX1BP1 in complex with NAP1, which not only uncover the mechanistic bases underpinning the specific interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1 but also reveal the binding mode of a SKICH domain. Moreover, we uncovered that the SKICH domains of NDP52 and TAX1BP1 share a general binding mode to interact with NAP1. Finally, we also evaluated the currently known TBK1-mediated phosphorylation sites in the SKICH domains of NDP52 and TAX1BP1 on the basis of their interactions with NAP1. In all, our findings provide mechanistic insights into the interactions of NAP1 with NDP52 and TAX1BP1, and are valuable for further understanding the functions of these proteins in selective autophagy.

PubMed: 30459273
DOI: 10.1073/pnas.1811421115

実験手法

X-RAY DIFFRACTION (2.301 Å)