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Impact of the Recent Mouse P‐Glycoprotein Structure for Structure‐Based Ligand Design
Author(s) -
Klepsch Freya,
Ecker Gerhard F.
Publication year - 2010
Publication title -
molecular informatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.481
H-Index - 68
eISSN - 1868-1751
pISSN - 1868-1743
DOI - 10.1002/minf.201000017
Subject(s) - p glycoprotein , transporter , efflux , multiple drug resistance , computational biology , transmembrane protein , drug resistance , drug , cheminformatics , ligand (biochemistry) , atp binding cassette transporter , chemistry , biology , pharmacology , biochemistry , bioinformatics , gene , genetics , receptor
P‐Glycoprotein (P‐gp), a transmembrane, ATP‐dependent drug efflux transporter, has attracted considerable interest both with respect to its role in tumour cell multidrug resistance and in absorption‐distribution and elimination of drugs. Although known since more than 30 years, the understanding of the molecular basis of drug/transporter interaction is still limited, which is mainly due to the lack of structural information available. However, within the past decade X‐ray structures of several bacterial homologues as well as very recently also of mouse P‐gp have become available. Within this review we give an overview on the current status of structural information available and on its impact for structure‐based drug design.