Preparation and crystallization of the disulfide-linked HLA-G dimer

Mitsunori Shiroishi, Daisuke Kohda, Katsumi Maenaka

    Research output: Contribution to journalArticlepeer-review

    7 Citations (Scopus)


    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 languageEnglish
    Pages (from-to)985-988
    Number of pages4
    JournalBiochimica et Biophysica Acta - Proteins and Proteomics
    Issue number5
    Publication statusPublished - May 2006

    All Science Journal Classification (ASJC) codes

    • Analytical Chemistry
    • Biophysics
    • Biochemistry
    • Molecular Biology


    Dive into the research topics of 'Preparation and crystallization of the disulfide-linked HLA-G dimer'. Together they form a unique fingerprint.

    Cite this