Journal:Acta Cryst D:S2059798320015004
From Proteopedia
(Difference between revisions)
| Line 7: | Line 7: | ||
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. | 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. | ||
| + | |||
| + | <scene name='86/869944/Cv/3'>The computational docking of TCA</scene> in the PDB entry [[4n7x]]. TCA molecule (cyan stick) docked into the outward-facing central cavity viewed from the extracellular side. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 14:38, 16 December 2020
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
