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  • Title: [Effects of induced deletion of repeats in binding domain of the VLDL receptor on its ligand-binding capacity].
    Author: Liu ZG, Qu S, Feng N, Zong YQ, Deng YZ, Feng ZC.
    Journal: Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai); 2002 Mar; 34(2):158-64. PubMed ID: 12006989.
    Abstract:
    The ligand-binding domain of the very low-density lipoprotein receptor (VLDL-R) contains eight cysteine-rich repeat sequences that have been postulated as ligand-binding sites. This is obviously different from that of low-density lipoprotein receptor (LDL-R) that includes seven similar repeats. To make clear the contribution of these repeats to ligand-binding and to explore the reason of both receptors' ligand-binding characteristic, the VLDL-R recombinants lacking different repeat(s) were constructed by oligonucleotide-directed mutagenesis and transfected into ldl-A7 cell. Ligand-binding results showed that repeat 1 and repeat 2 were the most important in binding with apoE-rich lipoprotein(VLDL and beta-VLDL). Repeat 3 and repeat 6 also important for binding VLDL. The results also showed that VLDL-R lacking LBR7 retained partly LDL-R ligand-binding properties. It suggests that LBR7 in VLDL-R may responsible for both receptors' ligand-binding properties differences.
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