par Abskharon, Romany N N;Soror, Sameh Hamdy;Pardon, Els;El Hassan, Hassan;Legname, Giuseppe;Steyaert, Jan;Wohlkonig, Alexandre 
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 66, 12, page (1644-1646)
Publication Publié, 2010-12
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 66, 12, page (1644-1646)
Publication Publié, 2010-12
Article révisé par les pairs
| Résumé : | Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrP C into the pathogenic isoform PrP Sc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dromedary heavy-chain antibodies) or nanobodies are single-domain antibodies, making them the smallest antigen-binding fragments. A specific nanobody (Nb-PrP-01) was raised against mouse PrP C. A crystallization condition for this recombinant nanobody was identified using high-throughput screening. The crystals were optimized using streak-seeding and the hanging-drop method. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 30.04, b = 37.15, c = 83.00 Å, and diffracted to 1.23 Å resolution using synchrotron radiation. The crystal structure of this specific nanobody against PrP C together with the known PrP C structure may help in understanding the PrP C/PrP Sc transition mechanism. © 2010 International Union of Crystallography. All rights reserved. |
