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 journalArticle

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

Fingerprint

Crystallization
X-Ray Diffraction
X ray diffraction analysis
Immunoglobulins
Non-Receptor Type 11 Protein Tyrosine Phosphatase
SH2 Domain-Containing Protein Tyrosine Phosphatases
crystallization
diffraction
Escherichia coli
Dilution
Tyrosine
Protein Phosphatase 2
Membrane Proteins
Protein Tyrosine Phosphatases
phosphatases
x rays
tyrosine
Chemical activation
Inclusion Bodies
Vapors

All Science Journal Classification (ASJC) codes

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

Cite this

Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα). / Tabata, Shigekazu; Kuroki, Kimiko; Maita, Nobuo; Wang, Jing; Shiratori, Ikuo; Arase, Hisashi; Kohda, Daisuke; Maenaka, Katsumi.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64, No. 1, 01.01.2008, p. 44-46.

Research output: Contribution to journalArticle

Tabata, Shigekazu ; Kuroki, Kimiko ; Maita, Nobuo ; Wang, Jing ; Shiratori, Ikuo ; Arase, Hisashi ; Kohda, Daisuke ; Maenaka, Katsumi. / Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα). In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2008 ; Vol. 64, No. 1. pp. 44-46.
@article{b3681271f6e142c0a727ee6962c9744e,
title = "Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα)",
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 {\AA} 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 {\AA}, and contain one molecule per asymmetric unit.",
author = "Shigekazu Tabata and Kimiko Kuroki and Nobuo Maita and Jing Wang and Ikuo Shiratori and Hisashi Arase and Daisuke Kohda and Katsumi Maenaka",
year = "2008",
month = "1",
day = "1",
doi = "10.1107/S1744309107065384",
language = "English",
volume = "64",
pages = "44--46",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "1",

}

TY - JOUR

T1 - Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα)

AU - Tabata, Shigekazu

AU - Kuroki, Kimiko

AU - Maita, Nobuo

AU - Wang, Jing

AU - Shiratori, Ikuo

AU - Arase, Hisashi

AU - Kohda, Daisuke

AU - Maenaka, Katsumi

PY - 2008/1/1

Y1 - 2008/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=37549036760&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37549036760&partnerID=8YFLogxK

U2 - 10.1107/S1744309107065384

DO - 10.1107/S1744309107065384

M3 - Article

C2 - 18097101

AN - SCOPUS:37549036760

VL - 64

SP - 44

EP - 46

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 1

ER -