The LDL Receptor Gene: A Mosaic of Exons Shared with Different Proteins

Thomas C. Südhof(The University of Texas Southwestern Medical Center), Joseph L. Goldstein(The University of Texas Southwestern Medical Center), Michael S. Brown(The University of Texas Southwestern Medical Center), David W. Russell(The University of Texas Southwestern Medical Center)
Science
May 17, 1985
Cited by 854Open Access
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Abstract

The multifunctional nature of coated pit receptors predicts that these proteins will contain multiple domains. To establish the genetic basis for these domains (LDL) receptor. This gene is more than 45 kilobases in length and contains 18 exons, most of which correlate with functional domains previously defined at the protein level. Thirteen of the 18 exons encode protein sequences that are homologous to sequences in other proteins: five of these exons encode a sequence similar to one in the C9 component of complement; three exons encode a sequence similar to a repeat sequence in the precursor for epidermal growth factor (EGF) and in three proteins of the blood clotting system (factor IX, factor X, and protein C); and five other exons encode nonrepeated sequences that are shared only with the EGF precursor. The LDL receptor appears to be a mosaic protein built up of exons shared with different proteins, and it therefore belongs to several supergene families.


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