Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

Nazzareno Dimasi, Manfred Roessle, Oscar Moran, Giovanni Candiano, Dmitri I. Svergun, Roberto Biassoni

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Natural killer (NK) cells are lymphocytes of the innate immune system specialized in recognition and killing of certain virus-infected and tumor cells. To carry out this task, NK cells are equipped with a complex array of germ line encoded receptors. These receptors deliver either positive or negative signals, and a delicate balance between these signals governs the NK cell cytolytic activity against the target cell. IRp60 (CD300a) is a human NK inhibitory receptor with an immunoglobulin-like fold. In the present study the IRp60 protein was expressed in Escherichia coli as inclusion bodies and refolded by dilution. The refolded protein was purified to homogeneity, biochemical characterized and the solution structure was investigated using small-angle X-ray scattering (SAXS). The SAXS data revealed that IRp60 is monomeric in solution with a molecular shape characteristic of the immunoglobulin-like structures. A homology model of IRp60 was built and validated experimentally against the SAXS data.

Original languageEnglish
Pages (from-to)193-200
Number of pages8
JournalInternational Journal of Biological Macromolecules
Volume40
Issue number3
DOIs
Publication statusPublished - Feb 28 2007

Fingerprint

KIR Receptors
X ray scattering
Natural Killer Cells
X-Rays
Immunoglobulins
Protein Refolding
Oncogenic Viruses
Lymphocytes
Immune system
Inclusion Bodies
Viruses
Germ Cells
Escherichia coli
Dilution
Tumors
Immune System
Proteins
Cells

Keywords

  • Homology modeling
  • Natural killer cell receptors
  • Protein expression and purification
  • Small-angle X-ray scattering
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a). / Dimasi, Nazzareno; Roessle, Manfred; Moran, Oscar; Candiano, Giovanni; Svergun, Dmitri I.; Biassoni, Roberto.

In: International Journal of Biological Macromolecules, Vol. 40, No. 3, 28.02.2007, p. 193-200.

Research output: Contribution to journalArticle

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