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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states
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Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

机译：四个人类LLT1的晶体结构,配体在各种不同的糖基化和人类NKR-P1齐聚反应状态

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摘要

Human LLT1 is a C-type lectin-like ligand of NKR-P1 (CD161, gene KLRB1), a C-type lectin-like receptor of natural killer cells. Using X-ray diffraction, the first experimental structures of human LLT1 were determined. Four structures of LLT1 under various conditions were determined: monomeric, dimeric deglycosylated after the first N-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc2Man5 glycosylation. The dimeric form follows the classical dimerization mode of human CD69. The monomeric form keeps the same fold with the exception of the position of an outer part of the long loop region. The hexamer of glycosylated LLT1 consists of three classical dimers. The hexameric packing may indicate a possible mode of interaction of C-type lectin-like proteins in the glycosylated form.
机译：人类LLT1这种lectin-like配体NKR-P1 (CD161基因KLRB1), c -型lectin-like自然杀伤细胞的受体。衍射,第一个实验的结构人类LLT1测定。LLT1在不同条件下测定:单体、二聚的deglycosylated后第一个N-acetylglucosamine单元在两种形式与齐次hexameric GlcNAc2Man5糖基化。人类CD69的经典二聚作用模式。单体的形式在褶皱的保持不变除了外部的一部分的位置长循环区域。LLT1包括三个经典的二聚体。hexameric包装可能表明一个可能的模式这种lectin-like蛋白质的相互作用糖基化的形式。

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