3S7X

Unassembled Washington University Polyomavirus VP1 Pentamer R198K Mutant

3S7X の概要

• エントリーDOI: 10.2210/pdb3s7x/pdb
• 関連するPDBエントリー: 1VPS 3BWR 3NXG 3S7V
• 分子名称: Major capsid protein VP1, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: jelly-roll fold, antiparallel beta sandwich, major capsid protein, viral protein
• 由来する生物種: WU Polyomavirus
• 細胞内の位置: Virion: A5HBD5
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 145867.14

構造登録者

Neu, U.,Wang, J.,Stehle, T. (登録日: 2011-05-27, 公開日: 2011-06-29, 最終更新日: 2024-11-06)

主引用文献

Neu, U.,Wang, J.,Macejak, D.,Garcea, R.L.,Stehle, T.
Structures of the major capsid proteins of the human KI and WU polyomaviruses.
J.Virol., 85:7384-7392, 2011

PubMed Abstract: The Karolinska Institutet and Washington University polyomaviruses (KIPyV and WUPyV, respectively) are recently discovered human viruses that infect the respiratory tract. Although they have not yet been linked to disease, they are prevalent in populations worldwide, with initial infection occurring in early childhood. Polyomavirus capsids consist of 72 pentamers of the major capsid protein viral protein 1 (VP1), which determines antigenicity and receptor specificity. The WUPyV and KIPyV VP1 proteins are distant in evolution from VP1 proteins of known structure such as simian virus 40 or murine polyomavirus. We present here the crystal structures of unassembled recombinant WUPyV and KIPyV VP1 pentamers at resolutions of 2.9 and 2.55 Å, respectively. The WUPyV and KIPyV VP1 core structures fold into the same β-sandwich that is a hallmark of all polyomavirus VP1 proteins crystallized to date. However, differences in sequence translate into profoundly different surface loop structures in KIPyV and WUPyV VP1 proteins. Such loop structures have not been observed for other polyomaviruses, and they provide initial clues about the possible interactions of these viruses with cell surface receptors.

PubMed: 21543504
DOI: 10.1128/JVI.00382-11

実験手法

X-RAY DIFFRACTION (2.9 Å)