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

被引:14
作者
Dimasi, N
Moretta, A
Moretta, L
Biassoni, R
Mariuzza, RA
机构
[1] Ist Giannina Gaslini, I-16147 Genoa, Italy
[2] Univ Genoa, Dipartimento Med Sperimentale, Sez Istol, I-16132 Genoa, Italy
[3] Univ Genoa, Dipartimento Med Sperimentale, Sez Patal Gernerale, I-16132 Genoa, Italy
[4] Ctr Adv Res Biotechnol, Rockville, MD 20850 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2004年 / 60卷
关键词
D O I
10.1107/S0907444903028439
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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 Angstrom, alpha = gamma = 90, beta = 113degrees. 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.
引用
收藏
页码:401 / 403
页数:3
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