1FOD

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

Summary for 1FOD

• Entry DOI: 10.2210/pdb1fod/pdb
• Descriptor: FOOT AND MOUTH DISEASE VIRUS, ... (4 entities in total)
• Functional Keywords: virus, icosahedral virus
• Biological source: Foot-and-mouth disease virus; More
• Total number of polymer chains: 4
• Total formula weight: 80826.57

Authors

Logan, D.T.,Lea, S.,Lewis, R.,Stuart, D.,Fry, E. (deposition date: 1993-10-27, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)