Preparation and crystallization of the disulfide-linked HLA-G dimer.
Biochim Biophys Acta
; 1764(5): 985-8, 2006 May.
Article
em En
| MEDLINE
| ID: mdl-16290109
ABSTRACT
HLA-G is a non-classical MHC class I, which binds to inhibitory receptors, such as Leukocyte Ig-like receptors, to induce a wide range of tolerogenic immunological effects. HLA-G can be expressed as a disulfide-liked dimer both in solution and at the cell surface. However, the three-dimensional structure of the HLA-G dimer is unknown. Here, we report the crystallization of the disulfide-linked dimer form of HLA-G by adding dithiothreitol (DTT), enabling a 3.2-A data set to be collected. We also show that DTT promotes disulfide bond exchange of refolded HLA-G, whose free cysteine was protected, thus facilitating its dimerization. This technique could also be applied for disulfide-mediated dimer/multimer formation of refolded proteins harbouring free cysteines.
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Base de dados:
MEDLINE
Assunto principal:
Antígenos de Histocompatibilidade Classe I
/
Dissulfetos
/
Antígenos HLA
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article