Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis
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The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding DomainsEnergy transduction and alternating access of the mammalian ABC transporter P-glycoprotein.Catalytic and transport cycles of ABC exporters.Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics.Mechanism Underlying the Reversal of Drug Resistance in P-Glycoprotein-Expressing Leukemia Cells by Pinoresinol and the Study of a DerivativeConformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter.Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus.An asymmetric post-hydrolysis state of the ABC transporter ATPase dimer.P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends.Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingMolecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded stateStructural characterization of two metastable ATP-bound states of P-glycoprotein.Kinetic validation of the models for P-glycoprotein ATP hydrolysis and vanadate-induced trapping. Proposal for additional steps.Reaction chemistry ABC-style.Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy.The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely togetherA single active catalytic site is sufficient to promote transport in P-glycoproteinConverting nonhydrolyzable nucleotides to strong cystic fibrosis transmembrane conductance regulator (CFTR) agonists by gain of function (GOF) mutationsExploring conformational equilibria of a heterodimeric ABC transporter.Marine natural products with P-glycoprotein inhibitor properties.Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity.Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.Unidirectional Transport Mechanism in an ATP Dependent Exporter.ABC transporters, mechanisms and biology: an overview.The P-glycoprotein multidrug transporter.Mechanism of the ABC transporter ATPase domains: catalytic models and the biochemical and biophysical record.The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoproteinCysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.Analyzing conformational dynamics of single P-glycoprotein transporters by Förster resonance energy transfer using hidden Markov models.Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein.The reliability of molecular dynamics simulations of the multidrug transporter P-glycoprotein in a membrane environment.Solid-state NMR and EPR Spectroscopy of Mn2+ -Substituted ATP-Fueled Protein Engines.Substrate versus inhibitor dynamics of P-glycoprotein.Allosteric effects of ATP binding on the nucleotide-binding domain of a heterodimeric ATP-binding cassette transporter.Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1.Allosteric Role of Substrate Occupancy Toward the Alignment of P-glycoprotein Nucleotide Binding Domains
P2860
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P2860
Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Characterization of an asymmet ...... es: implications for catalysis
@ast
Characterization of an asymmet ...... es: implications for catalysis
@en
type
label
Characterization of an asymmet ...... es: implications for catalysis
@ast
Characterization of an asymmet ...... es: implications for catalysis
@en
prefLabel
Characterization of an asymmet ...... es: implications for catalysis
@ast
Characterization of an asymmet ...... es: implications for catalysis
@en
P2093
P2860
P356
P1476
Characterization of an asymmet ...... es: implications for catalysis
@en
P2093
Alena Siarheyeva
Frances J Sharom
Ronghua Liu
P2860
P304
P356
10.1074/JBC.M109.047290
P407
P577
2010-01-08T00:00:00Z