Journal:Acta Cryst D:S2059798320015004
From Proteopedia
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Apical sodium-dependent bile acid transporter (ASBT) recycles bile acids from small intestine into enterocytes, and is a potential drug target for treating several metabolic diseases including type 2 diabetes. However, where and how bile acids bind in ASBT is unknown, which hampers our understanding toward its working mechanism. | Apical sodium-dependent bile acid transporter (ASBT) recycles bile acids from small intestine into enterocytes, and is a potential drug target for treating several metabolic diseases including type 2 diabetes. However, where and how bile acids bind in ASBT is unknown, which hampers our understanding toward its working mechanism. | ||
| - | In this study, four structures of an ASBT protein, called | + | In this study, four structures of an ASBT protein, called ASBT<sub>Yf</sub>, are determined. In these structures, several ligand-like acid molecules, including a citrate, a glycine and a sulfate, bind in a putative substrate-binding pocket of the protein. The structural data are consistent with a computational model the defines the substrate-binding site, and support the binding pattern of bile acids. Functional analysis further validates the computational bile acid binding model, which provides structural insights toward its transport mechanism. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:10, 16 December 2020
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