Identification of putative steroid-binding sites in human ABCB1 and ABCG2

Sergio Mares-Sámano, Raj Badhan, Jeffrey Penny

Research output: Contribution to journalArticle

Abstract

Homology modelling was used to generate three-dimensional structures of the nucleotide-binding domains (NBDs) of human ABCB1 and ABCG2. Interactions between a series of steroidal ligands and transporter NBDs were investigated using an in silico docking approach. C-terminal ABCB1 NBD (ABCB1 NBD2) was predicted to bind steroids within a cavity formed partly by the P-Loop, Tyr1044 and Ile1050. The P-Loop within ABCG2 NBD was also predicted to be involved in steroid binding. No overlap between ATP- and RU-486-binding sites was predicted in either NBD, though overlaps between ATP- and steroid-binding sites were predicted in the vicinity of the P-Loop in both nucleotide-binding domains.
LanguageEnglish
Pages3601-3611
Number of pages11
JournalEuropean Journal of Medicinal Chemistry
Volume44
Issue number9
Early online date6 Mar 2009
DOIs
Publication statusPublished - Sep 2009

Fingerprint

Nucleotides
Steroids
Binding Sites
Adenosine Triphosphate
Mifepristone
Computer Simulation
Ligands

Keywords

  • ABCB1
  • ABCG2
  • homology modelling
  • steroid
  • nucleotide-binding domain

Cite this

Mares-Sámano, Sergio ; Badhan, Raj ; Penny, Jeffrey. / Identification of putative steroid-binding sites in human ABCB1 and ABCG2. In: European Journal of Medicinal Chemistry. 2009 ; Vol. 44, No. 9. pp. 3601-3611.
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Identification of putative steroid-binding sites in human ABCB1 and ABCG2. / Mares-Sámano, Sergio; Badhan, Raj; Penny, Jeffrey.

In: European Journal of Medicinal Chemistry, Vol. 44, No. 9, 09.2009, p. 3601-3611.

Research output: Contribution to journalArticle

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