Mutational analysis of the ligand binding domain of the low density lipoprotein receptor.

作者: V Esser , L E Limbird , M S Brown , J L Goldstein , D W Russell

DOI: 10.1016/S0021-9258(18)37702-0

关键词:

摘要: The ligand binding domain of the low density lipoprotein (LDL) receptor contains seven imperfect repeats a 40-amino acid cysteine-rich sequence. Each repeat clustered negative charges that have been postulated as ligand-binding sites. adjacent region protein, growth factor homology region, three (A-C) whose sequence differs from those in domain. To dissect contribution these different to binding, we used oligonucleotide-directed mutagenesis alter expressible cDNAs for human LDL which were then introduced into monkey COS cells by transfection. We measured ability mutant receptors bind LDL, single protein (apoB-100), and beta-migrating very (beta-VLDL), apoB-100 plus multiple copies another (apoE). results show 1 is not required either ligand. Repeats 2 3 6 7 are maximal but beta-VLDL. Repeat 5 both ligands. A B binding. These support model various play additive roles each making separate event.

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