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Permanent link (DOI): https://doi.org/10.7939/R35D8NT7K

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

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Author or creator
Baral, Pravas K.
Wieland, Barbara
Swayampakula, Mridula
Polymenidou, Magdalini
Aguzzi, Adriano
Kav, Nat N. V.
James, Michael N. G.
Additional contributors
Subject/Keyword
Antibodies
Prions
POM1
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
Prion diseases are neurodegenerative diseases that are characterized by the con­version of the cellular prion protein PrPc to the pathogenic isoform PrPsc. 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°.
Date created
2011
DOI
doi:10.7939/R35D8NT7K
License information
© 2011 International Union of Crystallography. All rights reserved
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Citation for previous publication
Baral, P. K., Wieland, B., Swayampakula, M., Polymenidou, M., Aguzzi, A., Kav, N. N. V., & James, M. N. G. (2011). Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody. Acta Crystallographica Section F: Structural Biology Communications, 67(10), 1211-1213.  http://dx.doi.org/10.1107/S1744309111026273

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