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-Å 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.
Original language | English |
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Pages (from-to) | 985-988 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
Volume | 1764 |
Issue number | 5 |
DOIs | |
Publication status | Published - May 1 2006 |
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Biophysics
- Biochemistry
- Molecular Biology