2QIJ

Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.

2QIJ の概要

• エントリーDOI: 10.2210/pdb2qij/pdb
• 関連するPDBエントリー: 1QGT 2G33 2G34
• 分子名称: Core antigen (1 entity in total)
• 機能のキーワード: viral capsid protein, icosahedral virus, virus
• 由来する生物種: Hepatitis B virus subtype adyw
• 細胞内の位置: Virion : P03147
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70985.03

構造登録者

Tan, W.S.,McNae, I.W.,Ho, K.L.,Walkinshaw, M.D. (登録日: 2007-07-04, 公開日: 2007-12-11, 最終更新日: 2024-10-30)

主引用文献

Tan, W.S.,McNae, I.W.,Ho, K.L.,Walkinshaw, M.D.
Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension.
Acta Crystallogr.,Sect.F, 63:642-647, 2007

PubMed Abstract: Hepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20,000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 A resolution and data were collected to 99.6% completeness at 8.9 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 A. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells.

PubMed: 17671358
DOI: 10.1107/S1744309107033726

実験手法

X-RAY DIFFRACTION (8.9 Å)