2K9H

The hantavirus glycoprotein G1 tail contains a dual CCHC-type classical zinc fingers

2K9H の概要

• エントリーDOI: 10.2210/pdb2k9h/pdb
• 分子名称: Glycoprotein, ZINC ION (2 entities in total)
• 機能のキーワード: hantavirus, glycoprotein, zinc finger, cchc, metal binding protein
• 由来する生物種: Andes virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6475.06

構造登録者

Estrada, D.F.,Boudreaux, D.M.,Zhong, D.,St Jeor, S.C.,De Guzman, R.N. (登録日: 2008-10-13, 公開日: 2009-01-27, 最終更新日: 2024-05-22)

主引用文献

Estrada, D.F.,Boudreaux, D.M.,Zhong, D.,St Jeor, S.C.,De Guzman, R.N.
The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers.
J.Biol.Chem., 284:8654-8660, 2009

PubMed Abstract: Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction.

PubMed: 19179334
DOI: 10.1074/jbc.M808081200

実験手法

SOLUTION NMR