1fpt
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(New page: 200px<br /> <applet load="1fpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpt, resolution 3.0Å" /> '''THREE-DIMENSIONAL ST...)
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Revision as of 07:23, 18 November 2007
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THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN THE FAB FRAGMENT OF AN NEUTRALIZING ANTIBODY FOR TYPE 1 POLIOVIRUS AND ITS VIRAL EPITOPE
Overview
The crystal structure of the complex between the Fab fragment of C3, a, neutralizing antibody for poliovirus, and a peptide corresponding to the, viral epitope has been determined at 3.0 A resolution. Although this, antibody was originally raised to heat inactivated (noninfectious) virus, particles, it strongly neutralizes the Mahoney strain of type 1, poliovirus. Eleven peptide residues are well-defined in the, electron-density map and form two type I beta-turns in series. At the, carboxyl end, the peptide is bound snugly in the antibody-combining site, and adopts a conformation that differs significantly from the structure of, the corresponding residues in the virus. Structural comparisons between, the peptide in the complex and the viral epitope suggests that on binding, to infectious virions, this antibody may induce structural changes, important for neutralization.
About this Structure
1FPT is a Protein complex structure of sequences from Human poliovirus 1 and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the complex between the Fab fragment of a neutralizing antibody for type 1 poliovirus and its viral epitope., Wien MW, Filman DJ, Stura EA, Guillot S, Delpeyroux F, Crainic R, Hogle JM, Nat Struct Biol. 1995 Mar;2(3):232-43. PMID:7539711
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