Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT

Nien-Jen Hu, So Iwata (), Alexander D. Cameron () and David Drew ()
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Nien-Jen Hu: Imperial College London
So Iwata: Imperial College London
Alexander D. Cameron: Imperial College London
David Drew: Imperial College London

Nature, 2011, vol. 478, issue 7369, 408-411

Abstract: Structure of a bile acid transporter Elevated cholesterol levels significantly increase the risk of atherosclerosis and cardiovascular diseases. Cholesterol is eliminated from the body following conversion to bile acids, so the apical sodium-dependent bile acid transporter (ASBT) that reabsorbs bile acid in the intestine is a major drug target for cholesterol-lowering therapy. The X-ray crystal structure of a bacterial homologue of ASBT bound to its bile acid substrate has now been determined. The substrate (taurocholate) is found in a large hydrophobic cavity between the protein's 'core' and 'panel' domains, suggesting a possible transport mechanism for this important biomolecule.

Date: 2011
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DOI: 10.1038/nature10450

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