Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-51414
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 and Crystallization Communications, 67(Pt 10):1211-1213.
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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°.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology|
|DDC:||570 Life sciences; biology
610 Medicine & health
|Deposited On:||01 Dec 2011 11:38|
|Last Modified:||04 Dec 2013 09:34|
|Publisher:||International Union of Crystallography/Blackwell|
|Citations:||Web of Science®. Times Cited: 3|
Scopus®. Citation Count: 3
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