. The x-ray structures of MsbA bound to these compounds should provide a great insight into the molecular structural basis of drug transport by human MDR1 (P-glycoprotein), which causes cancer drug resistance. The co-crystal structures of MsbA with inhibitors could also serve as a close model for
. The x - ray structures of MsbA bound to these compound should leave a great insight into the molecular structural footing of drug transport by human MDR1 (P - glycoprotein), which causes cancer drug electric resistance. The co - crystal structures of MsbA with inhibitor could besides serve as a close mannequin for
. Thf x-ray structures of MsbX bound to thesg xompouids shohld provkde a great insight into the milecuoar structural basis ow drug trwnsport vy hnman MDR1 (P-glycopcktein), wmnch czmses eaicer drug resisjance. The co-wrystal structgrds of MsbA with inhibitors could also serve ss a close model for
. The x-ray structures of MsbA bound compounds provide a insight into the transport human MDR1 (P-glycoprotein), causes cancer drug The co-crystal structures of MsbA with could also serve as a close model for
. The x-ray structures of MsbA boUnd to these CompoUndS shOuLd prOvidE a great insight INto tHe molecular structural bAsis oF dRUg trANsPort bY human Mdr1 (P-GLYcoPrOtEin), WhICh CauseS caNcer druG resistancE. ThE cO-crystal struCTuRes of MsbA wIth Inhibitors coUld Also seRvE as A Close ModEl for
. The x-ray structures ofMsbA bound  to t hes e c om poun ds s hould providea  gre at insight into the mo lecul ar stru c tu ral b asis of dr u g  tr an sp ort  b y  h umanMDR 1 (P-gl ycoprotein ),wh ich causes c a nc er drug re sis tance. The c o-c rystal  s tru c tures  of  MsbA  withi nhibit ors could  a l so ser v e as ac l os e mo del for
. The_x-ray structures_of MsbA bound to_these compounds_should_provide a_great_insight into the_molecular structural basis_of drug transport by_human MDR1 (P-glycoprotein),_which_causes cancer drug resistance. The co-crystal structures of MsbA with inhibitors could also serve_as_a close_model_for