Crystal structure of the ectodomain of human transferrin receptor
Crystal structure of the ectodomain of human transferrin receptor
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DOI：
10.1126/science.286.5440.779
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发表时间：
1999-10-22
期刊：
影响因子：
56.9
通讯作者：
Harrison, SC
中科院分区：
文献类型：
--
作者：
Lawrence, CM;Ray, S;Harrison, SC
转铁蛋白受体（TfR）经历多轮网格蛋白介导的内吞作用并在细胞表面重新出现，输入负载铁的转铁蛋白（Tf）并在内体内排出铁后回收脱铁转铁蛋白。此处测定的人 TfR 二聚体胞外域的晶体结构分辨率为 3.2 埃，揭示了一个三域亚基。其中一个结构域与羧肽酶和氨肽酶非常相似，膜谷氨酸羧肽酶的特征可以从 TfR 结构中推断出来。提出了 Tf 与受体结合的模型。
The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure. A model is proposed for Tf binding to the receptor.