5FSG

Structure of the hantavirus nucleoprotein provides insights into the mechanism of RNA encapsidation and a template for drug design

5FSG の概要

• エントリーDOI: 10.2210/pdb5fsg/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900010
• 分子名称: MALTOSE-BINDING PERIPLASMIC PROTEIN, HANTAVIRUS NUCLEOPROTEIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (2 entities in total)
• 機能のキーワード: viral protein, nucleoprotein, nucleocapsid, virus, hantavirus, rna, encapsidation, korean hemorrhagic fever virus
• 由来する生物種: HANTAAN VIRUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78786.91

構造登録者

Olal, D.,Daumke, O. (登録日: 2016-01-05, 公開日: 2016-04-06, 最終更新日: 2024-10-23)

主引用文献

Olal, D.,Daumke, O.
Structure of the Hantavirus Nucleoprotein Provides Insights Into the Mechanism of RNA Encapsidation.
Cell Rep., 14:2092-, 2016

PubMed Abstract: Hantaviruses are etiological agents of life-threatening hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome. The nucleoprotein (N) of hantavirus is essential for viral transcription and replication, thus representing an attractive target for therapeutic intervention. We have determined the crystal structure of hantavirus N to 3.2 Å resolution. The structure reveals a two-lobed, mostly α-helical structure that is distantly related to that of orthobunyavirus Ns. A basic RNA binding pocket is located at the intersection between the two lobes. We provide evidence that oligomerization is mediated by amino- and C-terminal arms that bind to the adjacent monomers. Based on these findings, we suggest a model for the oligomeric ribonucleoprotein (RNP) complex. Our structure provides mechanistic insights into RNA encapsidation in the genus Hantavirus and constitutes a template for drug discovery efforts aimed at combating hantavirus infections.

PubMed: 26923588
DOI: 10.1016/J.CELREP.2016.02.005

実験手法

X-RAY DIFFRACTION (3.209 Å)