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 language | English |
---|---|
Pages (from-to) | 401-403 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 60 |
Issue number | 2 |
DOIs | |
Publication status | Published - Feb 2004 |
ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology