3J6O

Kinetic and Structural Analysis of Coxsackievirus B3 Receptor Interactions and Formation of the A-particle

3J6O の概要

• エントリーDOI: 10.2210/pdb3j6o/pdb
• 関連するPDBエントリー: 3J6L 3J6M 3J6N
• EMDBエントリー: 5927 5928
• 分子名称: Coxsackie and adenovirus receptor (1 entity in total)
• 機能のキーワード: coxsackievirus b3, cvb3, car, cell adhesion
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25046.23

構造登録者

Organtini, L.J.,Makhov, A.M.,Conway, J.F.,Hafenstein, S.,Carson, S.D. (登録日: 2014-03-19, 公開日: 2014-04-09, 最終更新日: 2024-10-16)

主引用文献

Organtini, L.J.,Makhov, A.M.,Conway, J.F.,Hafenstein, S.,Carson, S.D.
Kinetic and structural analysis of coxsackievirus b3 receptor interactions and formation of the a-particle.
J.Virol., 88:5755-5765, 2014

PubMed Abstract: The coxsackievirus and adenovirus receptor (CAR) has been identified as the cellular receptor for group B coxsackieviruses, including serotype 3 (CVB3). CAR mediates infection by binding to CVB3 and catalyzing conformational changes in the virus that result in formation of the altered, noninfectious A-particle. Kinetic analyses show that the apparent first-order rate constant for the inactivation of CVB3 by soluble CAR (sCAR) at physiological temperatures varies nonlinearly with sCAR concentration. Cryo-electron microscopy (cryo-EM) reconstruction of the CVB3-CAR complex resulted in a 9.0-Å resolution map that was interpreted with the four available crystal structures of CAR, providing a consensus footprint for the receptor binding site. The analysis of the cryo-EM structure identifies important virus-receptor interactions that are conserved across picornavirus species. These conserved interactions map to variable antigenic sites or structurally conserved regions, suggesting a combination of evolutionary mechanisms for receptor site preservation. The CAR-catalyzed A-particle structure was solved to a 6.6-Å resolution and shows significant rearrangement of internal features and symmetric interactions with the RNA genome.

PubMed: 24623425
DOI: 10.1128/JVI.00299-14

実験手法

ELECTRON MICROSCOPY (9 Å)