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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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Baral, Pravas K.
Kav, Nat N. V.
James, Michael N. G.
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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°.
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- © 2011 International Union of Crystallography. All rights reserved
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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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