Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy
about
Providing a molecular mechanism for P-glycoprotein; why would I bother?Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics.Intermediate structural states involved in MRP1-mediated drug transport. Role of glutathione.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 togetherConserved Walker A cysteines 431 and 1074 in human P-glycoprotein are accessible to thiol-specific agents in the apo and ADP-vanadate trapped conformations.Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.Cell discrimination by attenuated total reflection-Fourier transform infrared spectroscopy: the impact of preprocessing of spectra.ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transpoReplacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysisA new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter.The nucleotide-binding domains of P-glycoprotein. Functional symmetry in the isolated domain demonstrated by N-ethylmaleimide labelling.Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues.Conformational dynamics of P-glycoprotein in lipid nanodiscs and detergent micelles reveal complex motions on a wide time scale.Investigating the role of the invariant carboxylate residues E552 and E1197 in the catalytic activity of Abcb1a (mouse Mdr3).Allosteric Role of Substrate Occupancy Toward the Alignment of P-glycoprotein Nucleotide Binding Domains
P2860
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P2860
Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy
description
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im Februar 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/02/15)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/02/15)
@nl
наукова стаття, опублікована в лютому 2002
@uk
name
Structural and functional asym ...... ransform infrared spectroscopy
@ast
Structural and functional asym ...... ransform infrared spectroscopy
@en
Structural and functional asym ...... ransform infrared spectroscopy
@nl
type
label
Structural and functional asym ...... ransform infrared spectroscopy
@ast
Structural and functional asym ...... ransform infrared spectroscopy
@en
Structural and functional asym ...... ransform infrared spectroscopy
@nl
prefLabel
Structural and functional asym ...... ransform infrared spectroscopy
@ast
Structural and functional asym ...... ransform infrared spectroscopy
@en
Structural and functional asym ...... ransform infrared spectroscopy
@nl
P2093
P2860
P356
P1476
Structural and functional asym ...... ransform infrared spectroscopy
@en
P2093
Catherine Vigano
Isabelle Carrier
Jean-Marie Ruysschaert
Michel Julien
Philippe Gros
P2860
P304
P356
10.1074/JBC.M107928200
P407
P577
2002-02-15T00:00:00Z