Identification and characterisation of putative drug binding sites in human ATP-binding cassette B5 (ABCB5) transporter

Abstract The human ATP-binding cassette B5 (ABCB5) transporter, a member of the ABC transporter superfamily, is linked to chemoresistance in tumour cells by drug effluxion. However, little known about its structure and drug-binding sites. In this study, we generated an atomistic model full-length ABCB5 with highest quality using X-ray crystal mouse ABCB1 (Pgp1), close homologue well-studied family. Molecular dynamics simulations were used validate characterise structural properties cell membranes. docking substrates such as taxanes, anthracyclines, camptothecin etoposide then identify at least three putative binding sites for chemotherapeutic drugs transported ABCB5. location these predicted overlap corresponding Pgp1. These findings will serve basis future vitro studies nature identified substrate-binding transporter.