Crystal structure of the ectodomain of human transferrin receptor

被引：259

作者：

Lawrence, CM

Ray, S

Babyonyshev, M

Galluser, R

Borhani, DW

Harrison, SC

机构：

[1] Howard Hughes Med Inst, Boston, MA 02115 USA

[2] Childrens Hosp, Mol Med Lab, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

SCIENCE | 1999年 / 286卷 / 5440期

关键词：

D O I：

10.1126/science.286.5440.779

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：779 / 782

页数：4

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