| Literature DB >> 22102029 |
Pravas Kumar Baral1, Barbara Wieland, Mridula Swayampakula, Magdalini Polymenidou, Adriano Aguzzi, Nat N V Kav, Michael N G James.
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°.Entities:
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Year: 2011 PMID: 22102029 PMCID: PMC3212364 DOI: 10.1107/S1744309111026273
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091