Title : Structural Basis of Drug Recognition by the Multidrug Transporter ABCG2.

Pub. Date : 2021 Jun 25

PMID : 33838147






4 Functional Relationships(s)
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1 Here we present three cryo-EM structures of nanodisc-reconstituted, human ABCG2 bound to anticancer drugs tariquidar, topotecan and mitoxantrone. tariquidar ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
2 We observed that the binding pocket of ABCG2 can accommodate a single tariquidar molecule in a C-shaped conformation, similar to one of the two tariquidar molecules bound to ABCB1, where tariquidar acts as an inhibitor. tariquidar ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
3 We observed that the binding pocket of ABCG2 can accommodate a single tariquidar molecule in a C-shaped conformation, similar to one of the two tariquidar molecules bound to ABCB1, where tariquidar acts as an inhibitor. tariquidar ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
4 We observed that the binding pocket of ABCG2 can accommodate a single tariquidar molecule in a C-shaped conformation, similar to one of the two tariquidar molecules bound to ABCB1, where tariquidar acts as an inhibitor. tariquidar ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens