Expression and crystallographic characterization of the extracellular domain of human natural killer cell triggering receptor NKp46

Marco Ponassi, Claudia Cantoni, Roberto Biassoni, Romana Conte, Andrea Spallarossa, Alessandro Moretta, Lorenzo Moretta, Martino Bolognesi, Domenico Bordo

Research output: Contribution to journalArticle

Abstract

Human natural killer (NK) cells are regulated in their cytolytic activity by a delicate interplay between activating and inhibitory signals related to distinct families of triggering and inhibitory receptor proteins. NKp46 is a major NK cell-specific triggering receptor involved in the recognition and lysis of human and murine tumour and virally infected cells. It consists of an extracellular portion, composed of two Ig-like domains, a transmembrane segment and a small cytoplasmic domain. To shed light on the molecular-recognition events involved in NK cytotoxicity triggering mechanisms, the NKp46 extracellular region was cloned, overexpressed, refolded and crystallized. X-ray diffraction data could be collected to a resolution limit of 1.93 Å. Crystals of the NKp46 extracellular region belong to the hexagonal space group P61 (or P65), with unit-cell parameters a = b = 85.48, c = 59.91 Å, γ = 120°; the asymmetric unit contains one protein chain (197 amino acids).

Original languageEnglish
Pages (from-to)2259-2261
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
Issue number12
DOIs
Publication statusPublished - Dec 2003

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ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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