CRYSTAL-STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T-CELL CORECEPTOR CD8 AT 2.6 A-RESOLUTION
CRYSTAL-STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T-CELL CORECEPTOR CD8 AT 2.6 A-RESOLUTION
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DOI：
10.1016/0092-8674(92)90085-q
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发表时间：
1992-03-20
期刊：
影响因子：
64.5
通讯作者：
HENDRICKSON, WA
中科院分区：
文献类型：
--
作者：
LEAHY, DJ;AXEL, R;HENDRICKSON, WA
人CD 8-α细胞外部分的分泌片段已在CHO细胞中表达，该片段的去糖基化和蛋白水解形式已结晶。我们在这里报告的晶体结构，这一片段作为精制在2.6埃分辨率。使用来自免疫球蛋白轻链的10个可变结构域的叠加作为搜索模型，通过分子置换解析结构。在电子密度图中，仅CD 8-α的N-末端114个氨基酸可见。由这些残基形成的结构域具有免疫球蛋白可变结构域的典型折叠，并结合形成F（v）样同源二聚体。
A secreted fragment of the extracellular portion of human CD8-alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 angstrom resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8-alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form F(v)-Like homodimers.