Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 12): 1644-6, 2010 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-21139215
ABSTRACT
Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. 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 PrPC. 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 P2(1)2(1)2(1), with unit-cell parameters a=30.04, b=37.15, c=83.00â
Å, and diffracted to 1.23â
Å resolution using synchrotron radiation. The crystal structure of this specific nanobody against PrPC together with the known PrPC structure may help in understanding the PrPC/PrPSc transition mechanism.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Difração de Raios X
/
Príons
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Anticorpos
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Bélgica