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

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TitleStructure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1.
Publication TypeJournal Article
Year of Publication2004
AuthorsDimasi, N, Moretta, A, Moretta, L, Biassoni, R, Mariuzza, RA
JournalActa Crystallogr D Biol Crystallogr
Volume60
IssuePt 2
Pagination401-3
Date Published2004 Feb
ISSN0907-4449
KeywordsBinding Sites, Carbohydrates, Cloning, Molecular, Crystallography, X-Ray, Humans, Killer Cells, Natural, Models, Molecular, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Receptors, Immunologic
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 A 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 A, alpha = gamma = 90, beta = 113 degrees. 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.

DOI10.1107/S0907444903028439
Alternate JournalActa Crystallogr. D Biol. Crystallogr.
PubMed ID14747738
Grant ListAI47990 / AI / NIAID NIH HHS / United States