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Cover caption:

Front cover illustration: The polyprotein of foot-and-mouth disease virus (FMDV) is shown (boxed area), together with the site of the 2A/2B primary polyprotein cleavage site (arrow). Two aspects of the translational model of 2A-mediated 'cleavage' are shown below. In the complex shown on the left, the nascent 2A peptide (helix) contained within the exit tube of the ribosome is attached via the glycyl-tRNA (green) in the ribosomal P site. The C-terminal residues of 2A are proposed to reorient the glycyl-tRNA ester linkage to preclude it from nucleophilic attack by the prolyl-tRNA present in the ribosomal A site (yellow) – preventing peptide bond formation. Hydrolysis of the (2A) peptidyl-tRNA ester linkage releases the peptide from the complex. The complex on the right shows the subsequent translocation of the deacylated tRNA^Gly from the P to the E site and the prolyl-tRNA from the A to the P site, allowing the next aminoacyl-tRNA to enter the vacated A site. In this manner, the synthesis of the downstream 'cleavage' product may proceed – a 'pseudo-initiation'. The inset of the FMDV capsid structure is reproduced with kind permission of Professor D. Stuart, FRS. See the articles by M. L. L. Donnelly and others on pages 1013-1025 and 1027-1041.

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