Comparative Modelling of Organic Anion Transporting Polypeptides: Structural Insights and Comparison of Binding Modes.

ABSTRACT: To better understand the functionality of organic anion transporting polypeptides (OATPs) and to design new ligands, reliable structural data of each OATP is needed. In this work, we used a combination of homology model with molecular dynamics simulations to generate a comprehensive structural dataset, that encompasses a diverse set of OATPs but also their relevant conformations. Our OATP models share a conserved transmembrane helix folding harbouring a druggable binding pocket in the shape of an inner pore. Our simulations suggest that the conserved salt bridges at the extracellular region between residues on TM1 and TM7 might influence the entrance of substrates. Interactions between residues on TM1 and TM4 within OATP1 family shown their importance in transport of substrates. Additional

SUBMITTER: Tonduru AK 

PROVIDER: S-EPMC9738416 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature