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1FPT

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

Summary for 1FPT
Entry DOI10.2210/pdb1fpt/pdb
DescriptorFAB FRAGMENT OF AN NEUTRALIZING ANTIBODY FOR TYPE 1 POLIOVIRUS, IGG2A-KAPPA C3 FAB (LIGHT CHAIN), IGG2A-KAPPA C3 FAB (HEAVY CHAIN), ... (4 entities in total)
Functional Keywordscomplex (antibody-pv-1 fragment), complex (antibody-pv-1 fragment) complex, complex (antibody/pv-1 fragment)
Biological sourceHuman poliovirus 1
More
Cellular locationProtein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03299
Cell membrane; Single-pass membrane protein (Potential): P01865
Total number of polymer chains3
Total formula weight49499.09
Authors
Wien, M.W.,Hogle, J.M. (deposition date: 1995-01-26, release date: 1995-03-31, Last modification date: 2024-10-23)
Primary citationWien, M.W.,Filman, D.J.,Stura, E.A.,Guillot, S.,Delpeyroux, F.,Crainic, R.,Hogle, J.M.
Structure of the complex between the Fab fragment of a neutralizing antibody for type 1 poliovirus and its viral epitope.
Nat.Struct.Biol., 2:232-243, 1995
Cited by
PubMed Abstract: 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.
PubMed: 7539711
DOI: 10.1038/nsb0395-232
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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