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

Mitsunori Shiroishi, Daisuke Kohda, Katsumi Maenaka

研究成果: ジャーナルへの寄稿学術誌査読

7 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)985-988
ページ数4
ジャーナルBiochimica et Biophysica Acta - Proteins and Proteomics
1764
5
DOI
出版ステータス出版済み - 5月 2006

!!!All Science Journal Classification (ASJC) codes

  • 分析化学
  • 生物理学
  • 生化学
  • 分子生物学

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