1fod

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

Structural highlights 1fod is a 4 chain structure with sequence from Fmdv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

spinqualitylabelsall models 1fod, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image