Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα)

Shigekazu Tabata, Kimiko Kuroki, Nobuo Maita, Jing Wang, Ikuo Shiratori, Hisashi Arase, Daisuke Kohda, Katsumi Maenaka

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Human paired immunoglobulin-like (Ig-like) type 2 receptor α (PILRα) is a type I membrane protein that is mainly expressed in immune-related cells such as monocytes, granulocytes and dendritic cells. PILRα can suppress the functions of such immune cells because it has the immunoreceptor tyrosine-based inhibitory motif (ITIM) in the intracellular region, which recruits the phosphatase Src homology-2 (SH2) domain-containing protein tyrosine phosphatase 2 (SHP-2) to inhibit phophorylations induced by activation signals. The extracellular region of human PILRα comprises one immunoglobulin superfamily V-set domain and a stalk region. The V-set domain (residues 13-131) of human PILRα was overexpressed in Escherichia coli as inclusion bodies, refolded by rapid dilution and purified. The PILRα protein was successfully crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals diffracted to 1.3 Å resolution at SPring-8 BL41XU; they belong to space group P21212 1, with unit-cell parameters a = 40.4, b = 45.0, c = 56.9 Å, and contain one molecule per asymmetric unit.

Original languageEnglish
Pages (from-to)44-46
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number1
DOIs
Publication statusPublished - Jan 1 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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