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  • Title: Structural insight into an ankyrin-sensitive lipid-binding site of erythroid beta-spectrin.
    Author: Czogalla A, Jaszewski AR, Diakowski W, Bok E, Jezierski A, Sikorski AF.
    Journal: Mol Membr Biol; 2007; 24(3):215-24. PubMed ID: 17520478.
    Abstract:
    It was recently shown that the region within beta-spectrin responsible for interactions with ankyrin includes a lipid-binding site which displayed sensitivity to inhibition by ankyrin. We studied its structure by constructing a series of single and double spin-labeled beta-spectrin-derived peptides and analyzing their spin-spin distances via electron paramagnetic resonance spectroscopy and the Fourier deconvolution method. The results indicate that the whole ankyrin-sensitive lipid-binding site of beta-spectrin exhibits a helical conformation revealing a distinct 3(10)-helix contribution at its N-terminus. The start of the helix was located five residues upstream along the sequence compared to the theoretical predictions. A model based on the obtained data provides direct evidence that the examined lipid-binding site is a highly amphipathic helix, which is correlated with the specific conformation of its N-terminal fragment.
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