Abstract
The secondary structure of the TGR5 membrane-proximal C-terminus determines plasma membrane localization and responsiveness towards extracellular ligands
Highlights
TGR5 is a structurally unknown bile acid sensing [1] G protein-coupled receptor (GPCR)
Up to 18 amino acids of the membrane proximal C-terminus of TGR5 wildtype as well as of 8 different substitution and deletion variants within this region were subjected to molecular dynamics (MD) simulations of 600 ns length each using the Amber 11 suite of programs [4]
The most frequently occurring secondary structure in clusters 3 and 4 is a loop formation. These results show that an a-helix formation in the variants C-terminus is associated with a high functionality and membrane localization, as can be seen for clusters 1 and 5
Summary
TGR5 is a structurally unknown bile acid sensing [1] G protein-coupled receptor (GPCR). Up to 18 amino acids of the membrane proximal C-terminus of TGR5 wildtype as well as of 8 different substitution and deletion variants within this region were subjected to molecular dynamics (MD) simulations of 600 ns length each using the Amber 11 suite of programs [4]. These results show that an a-helix formation in the variants C-terminus is associated with a high functionality and membrane localization, as can be seen for clusters 1 and 5.
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