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首页> 外文期刊>Biochemistry >Identification of residues in CD6 which are critical for ligand binding.
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Identification of residues in CD6 which are critical for ligand binding.

机译:鉴定对配体结合至关重要的CD6中的残基。

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摘要

CD6 is a member of the scavenger receptor cysteine rich protein superfamily (SRCRSF). This family includes many cell surface proteins whose three-dimensional structures and functions are presently not well understood. The extracellular region of CD6 includes 3 SRCR domains. The membrane proximal SRCR domain specifically binds the activated leukocyte cell adhesion molecule (ALCAM), a CD6 ligand belonging to the immunoglobulin superfamily. CD6-ALCAM interactions mediate immune cell adhesion and are implicated in T cell maturation and the regulation of T cell function. On the basis of SRCRSF sequence comparison, a mutagenesis analysis of the membrane proximal SRCR domain of CD6 (CD6D3) has been carried out. Fifteen mutants were characterized. Three CD6 residues were identified in a region of low sequence conservation which, when mutated, abolish ligand binding but not the binding to a panel of conformationally sensitive anti-CD6 mAbs. This study provides the first analysis of residues critical for ligand binding to a member of the SRCRSF.
机译:CD6是清道夫受体富含半胱氨酸的蛋白质超家族(SRCRSF)的成员。该家族包括许多细胞表面蛋白,其三维结构和功能目前尚不十分清楚。 CD6的细胞外区域包括3个SRCR域。膜近端SRCR结构域特异性结合激活的白细胞粘附分子(ALCAM),ALCAM是属于免疫球蛋白超家族的CD6配体。 CD6-ALCAM相互作用介导免疫细胞粘附,并参与T细胞成熟和T细胞功能的调节。在SRCRSF序列比较的基础上,对CD6(CD6D3)的膜近端SRCR结构域进行了诱变分析。表征了十五个突变体。在低序列保守性的区域中鉴定出三个CD6残基,当突变时,该残基消除了配体结合,但不消除与一组构象敏感的抗CD6 mAb的结合。这项研究提供了对配体与SRCRSF成员结合至关重要的残基的首次分析。

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