Glutamine residues in Q-loops of multidrug resistance protein MRP1 contribute to ATP binding via interaction with metal cofactor

Article ID	Journal	Published Year	Pages	File Type
10797848	Biochimica et Biophysica Acta (BBA) - Biomembranes	2011	7 Pages	PDF

Abstract

âº The Q residues in Q-loops of MRP1 interact with Mg++ and contribute to MgÂ Â·Â ATP-binding. âº Mutations eliminating amide group significantly decreased MgÂ Â·Â ATP binding. âº Mutations eliminating amide group significantly increased the Km and Vmax values. âº The Q residues in Q-loops of MRP1 may not play a crucial role in ATP hydrolysis. âº May not play crucial roles in transmitting the conformational changes between domains.

Keywords

PBS Metal cofactor Sf21 MRP1 NBD LTC4 P-gp TMD Bcrp EGTA SDS ABC P-glycoprotein nucleotide binding domain transmembrane domain sodium dodecyl sulfate Leukotriene C4 Phosphate-buffered saline breast cancer resistance protein multidrug resistance protein 1 ATP binding cassette