1qgc
From Proteopedia
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STRUCTURE OF THE COMPLEX OF AN FAB FRAGMENT OF A NEUTRALIZING ANTIBODY WITH FOOT AND MOUTH DISEASE VIRUS
Overview
Data from cryo-electron microscopy and X-ray crystallography have been, combined to study the interactions of foot-and-mouth disease virus, serotype C (FMDV-C) with a strongly neutralizing monoclonal antibody (mAb), SD6. The mAb SD6 binds to the long flexible GH-loop of viral protein 1, (VP1) which also binds to an integrin receptor. The structure of the, virus-Fab complex was determined to 30 A resolution using cryo-electron, microscopy and image analysis. The known structure of FMDV-C, and of the, SD6 Fab co-crystallized with a synthetic peptide corresponding to the, GH-loop of VP1, were fitted to the cryo-electron microscope density map., The SD6 Fab is seen to project almost radially from the viral surface in, an orientation which is only compatible with monovalent binding of the, mAb. Even taking into account the mAb hinge and elbow flexibility, it is, not possible to model bivalent binding without severely distorting the, Fabs. The bound GH-loop is essentially in what has previously been termed, the 'up' position in the best fit Fab orientation. The SD6 Fab interacts, almost exclusively with the GH-loop of VP1, making very few other contacts, with the viral capsid. The position and orientation of the SD6 Fab bound, to FMDV-C is in accord with previous immunogenic data.
About this Structure
1QGC is a Protein complex structure of sequences from Foot-and-mouth disease virus - type c and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop., Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI, EMBO J. 1997 Apr 1;16(7):1492-500. PMID:9130694
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