Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1.
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.
Dimasi
Nazzareno
N
Istituto Giannina Gaslini, Largo Gerolamo Gaslini 5, 16147 Genova, Italy. ndimasi@email.it
Moretta
Alessandro
A
Moretta
Lorenzo
L
Biassoni
Roberto
R
Mariuzza
Roy A
RA
D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006801:Humans; D007694:Killer Cells, Natural / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011971:Receptors, Immunologic / Q000737:chemistry*
D002241:Carbohydrates; D011971:Receptors, Immunologic; C121772:adhesion inhibitory receptor molecule 1