6O5W

Crystal structure of MORC3 CW domain fused with viral influenza A NS1 peptide

6O5W の概要

• エントリーDOI: 10.2210/pdb6o5w/pdb
• 分子名称: NS1-linked peptide,MORC family CW-type zinc finger protein 3, ZINC ION (3 entities in total)
• 機能のキーワード: morc3, atpase, ns1, virus, histone, cw, chromatin, transcription
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6857.86

構造登録者

Ahn, J.,Zhang, Y.,Vann, K.R.,Kutateleadze, T. (登録日: 2019-03-04, 公開日: 2019-05-08, 最終更新日: 2023-10-11)

主引用文献

Zhang, Y.,Ahn, J.,Green, K.J.,Vann, K.R.,Black, J.,Brooke, C.B.,Kutateladze, T.G.
MORC3 Is a Target of the Influenza A Viral Protein NS1.
Structure, 27:1029-1033.e3, 2019

PubMed Abstract: Microrchidia 3 (MORC3), a human ATPase linked to several autoimmune disorders, has been characterized both as a negative and positive regulator of influenza A virus. Here, we report that the CW domain of MORC3 (MORC3-CW) is targeted by the C-terminal tail of the influenza H3N2 protein NS1. The crystal structure of the MORC3-CW:NS1 complex shows that NS1 occupies the same binding site in CW that is normally occupied by histone H3, a physiological ligand of MORC3-CW. Comparable binding affinities of MORC3-CW to H3 and NS1 peptides and to the adjacent catalytic ATPase domain suggest that the viral protein can compete with the host histone for the association with CW, releasing MORC3 autoinhibition and activating the catalytic function of MORC3. Our structural, biochemical, and cellular analyses suggest that MORC3 might affect the infectivity of influenza virus and therefore has a role in cell immune response.

PubMed: 31006586
DOI: 10.1016/j.str.2019.03.015

実験手法

X-RAY DIFFRACTION (1.412 Å)