What is it about?

To maximize host cell subversion, viruses often produce proteins lacking defined structure, otherwise known as disordered proteins. These proteins are like 'viral multi-tools', allowing viruses to appear in many different ways and attack many targets inside cells at once. These proteins are also challenging therapeutic targets since medicines typically need a structurally fixed binding site. In this report, we discuss how Hendra virus V protein binds human transporter proteins and adopts a fixed structure, potentially revealing a new therapeutic target. 宿主細胞の混乱を最大化するために、ウイルスはよく非構成化タンパク質を生産します。しかし、医薬は一般的にタンパク質の固定構造を結合するから、これらのタンパク質は治療目標として難しいです。本稿では、ヘンドラウイルス「V」タンパク質が固定構造を採用し、新しい治療標的を明らかにする方法について説明したい。

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This page is a summary of: Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V, Scientific Reports, January 2018, Springer Science + Business Media,
DOI: 10.1038/s41598-017-18742-8.
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