人类T细胞核受体CD8可溶性形式的晶体结构,分辨率为2.6A
D J Leahy1, R Axel, W A Hendrickson
1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Cell
|March 20, 1992
概括
研究人员结晶了人类CD8α片段,揭示了它的结构. 这个片段,包括N-终端114氨基酸,形成免疫球蛋白可变域类同位素.
科学领域:
- 结构生物学是结构生物学.
- 免疫学 免疫学 免疫学
- 蛋白质结晶学 蛋白质结晶学
背景情况:
- CD8α是一种细胞表面糖蛋白,对T细胞受体信号传递至关重要.
- 了解CD8α结构,可以了解免疫细胞相互作用.
研究的目的:
- 为了确定人体CD8α的分泌片段的晶体结构.
- 阐明CD8α细胞外域的结构特征和四级组织.
主要方法:
- 在中国仓鼠卵巢 (CHO) 细胞中分泌的CD8α片段的表达.
- 碎片的脱糖和蛋白质化形式的结晶.
- 在2.6A分辨率的X射线晶体学.
- 用免疫球蛋白轻链可变域作为搜索模型进行分子替代.
主要成果:
- 确定了CD8α的N端114氨基酸的晶体结构.
- 确定的域表现出免疫球蛋白可变域的折叠特征.
- 观察到CD8α片段与Fv类同型分子结合.
结论:
- 该结构揭示了CD8α细胞外N端区域的免疫球蛋白类折叠.
- 同型二元体的形成表明CD8α功能在T细胞相互作用中的潜在机制.
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