The human LDL receptor: A cysteine-rich protein with multiple Alu sequences in its mRNA

Tokuo Yamamoto, C. Geoffrey Davis, Michael S. Brown, Wolfgang J. Schneider, M. Linette Casey, Joseph L. Goldstein, David W. Russell

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Abstract

The nucleotide sequence of a cloned 5.3 kilobase cDNA for the human low density lipoprotein receptor revealed five domains in the 839 amino acid protein: 322 NH2-terminal amino acids, extremely rich in disulfide-bonded cysteine residues (15%) and including an 8-fold repeat of 40 residues that may contain the LDL binding site; 350 residues homologous to the precursor of mouse epidermal growth factor; a region immediately outside the plasma membrane, rich in serine and threonine and the site of O-linked glycosylation; 22 hydrophobic amino acids, spanning the plasma membrane; and 50 COOH-terminal amino acids, projecting into the cytoplasm. The mRNA for the receptor contains a 3′ untranslated region of 2.5 kilobases that includes multiple copies of the Alu family of repetitive DNAs. Transfection of simian COS cells with the human LDL receptor cDNA linked to the SV40 early promoter resulted in expression of functional cell surface receptors.

Original languageEnglish (US)
Pages (from-to)27-38
Number of pages12
JournalCell
Volume39
Issue number1
DOIs
StatePublished - Nov 1984

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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