Crystal structures of RAE-1β and its complex with the activating immunoreceptor NKG2D
Crystal structures of RAE-1β and its complex with the activating immunoreceptor NKG2D
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DOI：
10.1016/s1074-7613(02)00258-3
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发表时间：
2002-01-01
期刊：
影响因子：
32.4
通讯作者：
Strong, RK
中科院分区：
文献类型：
--
作者：
Li, PW;McDermott, G;Strong, RK
啮齿动物 RAE-1 蛋白由视黄酸诱导，在发育中发挥作用，是激活免疫受体 NKG2D 的配体，广泛表达于自然杀伤细胞、T 细胞和巨噬细胞上。 RAE-1 蛋白（α、β、γ 和 δ）是远距离主要组织相容性复合体 (MHC) I 类同源物，包含分离的 alpha1alpha2 平台域。 RAE-1beta 的晶体结构与其他 MHC 同系物不同，并显示出非规范的二硫键。通过疏水性、富含亮氨酸的界面，凹槽限定螺旋的紧密接近促进了肽结合凹槽的任何残余物的损失。 RAE-1β-鼠NKG2D复合物结构类似于人类NKG2D-MICA受体-配体复合物，并进一步证明了NKG2D配体结合位点的混杂性。
Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site.