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Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody.

Authors :
Baral PK
Wieland B
Swayampakula M
Polymenidou M
Aguzzi A
Kav NN
James MN
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2011 Oct 01; Vol. 67 (Pt 10), pp. 1211-3. Date of Electronic Publication: 2011 Sep 24.
Publication Year :
2011

Abstract

Prion diseases are neurodegenerative diseases that are characterized by the conversion of the cellular prion protein PrP(c) to the pathogenic isoform PrP(sc). Several antibodies are known to interact with the cellular prion protein and to inhibit this transition. An antibody Fab fragment, Fab POM1, was produced that recognizes a structural motif of the C-terminal domain of mouse prion protein. To study the mechanism by which Fab POM1 recognizes and binds the prion molecule, the complex between Fab POM1 and the C-terminal domain of mouse prion (residues 120-232) was prepared and crystallized. Crystals of this binary complex belonged to the monoclinic space group C2, with unit-cell parameters a = 83.68, b = 106.9, c = 76.25 Å, β = 95.6°.<br /> (© 2011 International Union of Crystallography. All rights reserved.)

Details

Language :
English
ISSN :
1744-3091
Volume :
67
Issue :
Pt 10
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
22102029
Full Text :
https://doi.org/10.1107/S1744309111026273