Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1

Nazzareno Dimasi, Alessandro Moretta, Lorenzo Moretta, Roberto Biassoni, Roy A. Mariuzza

Research output: Contribution to journalArticlepeer-review

Abstract

The high-resolution crystal structure of the functional N-terminal domain from the extracellular region of the human natural killer cell inhibitory receptor p75/AIRM1 or Siglec-7 has been determined at 1.45 Å resolution; it was obtained from a crystal belonging to a primitive monoclinic space group, with unit-cell parameters a = 32.65, b = 49.72, c = 39.79 Å, α = γ= 90, β = 113°. The structure reported here belongs to a different space group than the previously described Siglec-7 structure and was obtained using a bacterial expression system. The structure unveils the fine structural requirements adopted by a natural killer cell inhibitory receptor of the Siglec family in target-cell recognition and binding.

Original languageEnglish
Pages (from-to)401-403
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number2
DOIs
Publication statusPublished - Feb 2004

ASJC Scopus subject areas

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

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