1CN3

INTERACTION OF POLYOMAVIRUS INTERNAL PROTEIN VP2 WITH MAJOR CAPSID PROTEIN VP1 AND IMPLICATIONS FOR PARTICIPATION OF VP2 IN VIRAL ENTRY

1CN3 の概要

• エントリーDOI: 10.2210/pdb1cn3/pdb
• 分子名称: COAT PROTEIN VP1, FRAGMENT OF COAT PROTEIN VP2 (2 entities in total)
• 機能のキーワード: viral coat protein vp1, viral coat protein vp2, viral entry, viral protein
• 由来する生物種: Polyomavirus; 詳細
• 細胞内の位置: Virion: P49302; Isoform VP2: Virion. Isoform VP3: Virion: P12908
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 160305.21

構造登録者

Chen, X.,Stehle, T.,Harrison, S.C. (登録日: 1999-05-24, 公開日: 1999-06-09, 最終更新日: 2023-12-27)

主引用文献

Chen, X.S.,Stehle, T.,Harrison, S.C.
Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry.
EMBO J., 17:3233-3240, 1998

PubMed Abstract: A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli. A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VP1 pentamer, has been determined at 2.2 A resolution. The structure shows specific contacts between a single copy of the internal protein and a pentamer of VP1. These interactions were not detected in the previously described structure of the virion, but the location of VP2 in the recombinant complex is consistent with features in the virion electron-density map. The C-terminus of VP2/VP3 inserts in an unusual, hairpin-like manner into the axial cavity of the VP1 pentamer, where it is anchored strongly by hydrophobic interactions. The remainder of the internal protein appears to have significant flexibility. This structure restricts possible models for exposure of the internal proteins during viral entry.

PubMed: 9628860
DOI: 10.1093/emboj/17.12.3233

実験手法

X-RAY DIFFRACTION (2.2 Å)