EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes.
ジャーナル・号・ページ	J Virol, Vol. 79, Issue 12, Page 7745-7755, Year 2005
掲載日	2005年6月28日
著者	Doryen Bubeck / David J Filman / Naiqian Cheng / Alasdair C Steven / James M Hogle / David M Belnap /
PubMed 要旨	Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational ...Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational change to the 135S cell entry intermediate. This transition involves shifts of the capsid protein beta barrels, accompanied by the externalization of VP4 and the N terminus of VP1. Both polypeptides associate with membranes and are postulated to facilitate entry by forming a translocation pore for the viral RNA. We have calculated cryo-electron microscopic reconstructions of 135S particles that permit accurate placement of the beta barrels, loops, and terminal extensions of the capsid proteins. The reconstructions and resulting models indicate that each N terminus of VP1 exits the capsid though an opening in the interface between VP1 and VP3 at the base of the canyon that surrounds the fivefold axis. Comparison with reconstructions of 135S particles in which the first 31 residues of VP1 were proteolytically removed revealed that the externalized N terminus is located near the tips of propeller-like features surrounding the threefold axes rather than at the fivefold axes, as had been proposed in previous models. These observations have forced a reexamination of current models for the role of the 135S particle in transmembrane pore formation and suggest testable alternatives.
リンク	J Virol / PubMed:15919927 / PubMed Central
手法	EM (単粒子)
解像度	8.7 - 11.0 Å
構造データ	1133 1xyr EMDB-1133: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. PDB-1xyr: Poliovirus 135S cell entry intermediate 手法: EM (単粒子) / 解像度: 9.6 Å 1136 1xyr EMDB-1136: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. PDB-1xyr: Poliovirus 135S cell entry intermediate 手法: EM (単粒子) / 解像度: 8.7 Å 1137 1xyr EMDB-1137: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. PDB-1xyr: Poliovirus 135S cell entry intermediate 手法: EM (単粒子) / 解像度: 10.3 Å 1144 1xyr EMDB-1144: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. PDB-1xyr: Poliovirus 135S cell entry intermediate 手法: EM (単粒子) / 解像度: 11.0 Å 1145 1xyr EMDB-1145: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. PDB-1xyr: Poliovirus 135S cell entry intermediate 手法: EM (単粒子) / 解像度: 11.0 Å
由来	human poliovirus 1 (ポリオウイルス)
キーワード	VIRUS / BETA BARREL / VIRAL CAPSID / CELL ENTRY INTERMEDIATE / Icosahedral virus