1fpt: Difference between revisions

Revision as of 13:41, 21 February 2008

THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN THE FAB FRAGMENT OF AN NEUTRALIZING ANTIBODY FOR TYPE 1 POLIOVIRUS AND ITS VIRAL EPITOPE

OverviewOverview

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 StructureAbout this Structure

1FPT is a Protein complex structure of sequences from Human poliovirus 1 and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:41:19 2008

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 ==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.
+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==
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 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Hogle, J.M.]]
+[[Category: Hogle, J M.]]
-[[Category: Wien, M.W.]]
+[[Category: Wien, M W.]]
 [[Category: complex (antibody/pv-1 fragment)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:19 2008''