Literature DB >> 10531064

Crystal structure of the ectodomain of human transferrin receptor.

C M Lawrence1, S Ray, M Babyonyshev, R Galluser, D W Borhani, S C Harrison.   

Abstract

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.

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Year:  1999        PMID： 10531064     DOI： 10.1126/science.286.5440.779

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  103 in total

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