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Molecular modeling of the human multidrug resistance protein 1 (MRP1/ABCC1).

Abstract：

:Multidrug resistance protein 1 (MRP1/ABCC1) is a 190kDa member of the ATP-binding cassette (ABC) superfamily of transmembrane transporters that is clinically relevant for its ability to confer multidrug resistance by actively effluxing anticancer drugs. Knowledge of the atomic structure of MRP1 is needed to elucidate its transport mechanism, but only low resolution structural data are currently available. Consequently, comparative modeling has been used to generate models of human MRP1 based on the crystal structure of the ABC transporter Sav1866 from Staphylococcus aureus. In these Sav1866-based models, the arrangement of transmembrane helices differs strikingly from earlier models of MRP1 based on the structure of the bacterial lipid transporter MsbA, both with respect to packing of the twelve helices and their interactions with the nucleotide binding domains. The functional importance of Tyr324 in transmembrane helix 6 predicted to project into the substrate translocation pathway was investigated.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

DeGorter MK,Conseil G,Deeley RG,Campbell RL,Cole SP

doi

10.1016/j.bbrc.2007.10.141

subject

Has Abstract

pub_date

2008-01-04 00:00:00

pages

29-34

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02285-1

journal_volume

365

pub_type

杂志文章

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