Functional Interactions Between Nucleotide Binding Domains and Leukotriene C4 Binding Sites of Multidrug Resistance Protein 1 (ABCC1)

2005 ◽  
Vol 67 (6) ◽  
pp. 1944-1953 ◽  
Author(s):  
Lea Payen ◽  
Mian Gao ◽  
Christopher Westlake ◽  
Ashley Theis ◽  
Susan P. C. Cole ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
Multidrug Resistance Protein ◽  
Leukotriene C4 ◽  
Multidrug Resistance Protein 1 ◽  
Functional Interactions ◽  
Binding Domains ◽  
Resistance Protein

Residues Responsible for the Asymmetric Function of the Nucleotide Binding Domains of Multidrug Resistance Protein 1†

Biochemistry ◽  
2008 ◽  
Vol 47 (52) ◽  
pp. 13952-13965 ◽  
Author(s):  
Lei Qin ◽  
Jimin Zheng ◽  
Caroline E. Grant ◽  
Zongchao Jia ◽  
Susan P. C. Cole ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Nucleotide Binding ◽  
Multidrug Resistance Protein ◽  
Multidrug Resistance Protein 1 ◽  
Binding Domains ◽  
Resistance Protein ◽  
Asymmetric Function

scholarly journals Transport of leukotriene C4 by a cysteine-less multidrug resistance protein 1 (MRP1)

2003 ◽  
Vol 370 (1) ◽  
pp. 357-360 ◽  
Author(s):  
Sung H. LEE ◽  
Guillermo A. ALTENBERG
Keyword(s):  
Multidrug Resistance ◽  
Drug Transport ◽  
Transmembrane Domain ◽  
Low Cost ◽  
Expression System ◽  
Multidrug Resistance Protein ◽  
Leukotriene C4 ◽  
Multidrug Resistance Protein 1 ◽  
Yeast Expression System ◽  
Resistance Protein

Overexpression of multidrug resistance protein 1 (MRP1), an ATP-binding cassette protein, causes multidrug resistance. We developed a functional cysteine-less version of MRP1 that provides a framework for detailed biochemical and biophysical studies. The 18 Cys residues of a truncated MRP1 (tMRP1; lacking the first multispanning transmembrane domain) were replaced with Ala to generate Cys-less tMRP1 (CL tMRP1). CL tMRP1 expressed in Saccharomyces cerevisiae membranes displayed high-affinity ATP-dependent transport of the MRP1 substrate leukotriene C4. Compared with full-length MRP1, the Km for leukotriene C4 transport by CL tMRP1 was increased 3-fold, while Vmax was not affected. Thus a functional CL tMRP1 can be expressed using a low-cost and rapid-generation yeast expression system. This Cys-less protein can be used for biochemical, spectroscopic and structural studies to elucidate the mechanism of drug transport by MRP1.

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