Structural and functional aspects of the Ly49 natural killer cell receptors

被引:42
作者
Dimasi, N [1 ]
Biassoni, R [1 ]
机构
[1] Giannina Gaslinis Childrens Inst, Mol Med Lab, Genoa, Italy
关键词
activating receptor; crystal structure; immunoreceptor; inhibitory receptor; Ly49; Ly49/MHC complex; MHC class I; NK cell; NK cell receptor;
D O I
10.1111/j.1440-1711.2005.01301.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Natural killer cells are part of the first line of innate immune defence against virus-infected cells and cancer cells in the vertebrate immune system. They are called 'natural' killers because, unlike cytotoxic T cells, they do not require a previous challenge and preactivation to become active. The Ly49 NK receptors are type II transmembrane glycoproteins, structurally characterized as disulphide-linked homodimers. They share extensive homology with C-type lectins, and they are encoded by a multigene family that in mice maps on chromosome 6. A fine balance between inhibitory and activating signals regulates the function of NK cells. Inhibitory Ly49 molecules bind primarily MHC class I ligands, whereas the ligands for activating Ly49 molecules may include MHC class I, but also interestingly MHC class I-like molecules expressed by viruses, as is the case for Ly49H, which binds the m157 gene product of murine cytomegalovirus. In this study, we review the function and X-ray crystal structure of the Ly49 NK cell receptors hitherto determined (Ly49A, Ly49C and Ly49I), and the structural features of the Ly49/MHC class I interaction as revealed by the X-ray crystal structures of Ly49A/H-2D(d) and the recently determined Ly49C/H-2K(b).
引用
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页码:1 / 8
页数:8
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