1fod
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(New page: 200px<br /><applet load="1fod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fod, resolution 2.6Å" /> '''STRUCTURE OF A MAJOR ...)
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Revision as of 22:01, 24 November 2007
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STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS
Overview
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.
About this Structure
1FOD is a Protein complex structure of sequences from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.
Reference
Structure of a major immunogenic site on foot-and-mouth disease virus., Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J, Parry N, et al., Nature. 1993 Apr 8;362(6420):566-8. PMID:8385272
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