1FOD

STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS

1FOD の概要

• エントリーDOI: 10.2210/pdb1fod/pdb
• 分子名称: FOOT AND MOUTH DISEASE VIRUS, ... (4 entities in total)
• 機能のキーワード: virus, icosahedral virus
• 由来する生物種: Foot-and-mouth disease virus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 80826.57

構造登録者

Logan, D.T.,Lea, S.,Lewis, R.,Stuart, D.,Fry, E. (登録日: 1993-10-27, 公開日: 1994-01-31, 最終更新日: 2024-02-07)

主引用文献

Logan, D.,Abu-Ghazaleh, R.,Blakemore, W.,Curry, S.,Jackson, T.,King, A.,Lea, S.,Lewis, R.,Newman, J.,Parry, N.,Rowlands, D.,Stuart, D.,Fry, E.
Structure of a major immunogenic site on foot-and-mouth disease virus.
Nature, 362:566-568, 1993

PubMed Abstract: Attachment of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between beta-strands G and H of capsid protein VP1, was disordered and hence essentially invisible. We previously surmised that its disorder is enhanced by a disulphide bond linking the base of the loop (Cys 134) to Cys 130 of VP2 (ref. 8). We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological experiments suggest that some of the loop's internal structure is conserved. But here its structure has become sufficiently ordered to allow us to describe an unambiguous conformation, which we relate to some key biological properties of the virus.

PubMed: 8385272
DOI: 10.1038/362566a0

実験手法

X-RAY DIFFRACTION (2.6 Å)