Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site
about
Conformational motion of the ABC transporter MsbA induced by ATP hydrolysisFlexibility in the ABC transporter MsbA: Alternating access with a twist.Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains.Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites.Molecular models of human P-glycoprotein in two different catalytic statesStructure and function of efflux pumps that confer resistance to drugsIdentification and characterization of the binding sites of P-glycoprotein for multidrug resistance-related drugs and modulators.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 togetherThe translocation mechanism of P-glycoprotein.Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Bilayer mechanical properties regulate the transmembrane helix mobility and enzymatic state of CD39.Binding site of ABC transporter homology models confirmed by ABCB1 crystal structureIdentification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.Prediction of Therapy Response and Prognosis in Leukemias by Flow Cytometric MDR Assays.Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesisArginines in the first transmembrane segment promote maturation of a P-glycoprotein processing mutant by hydrogen bond interactions with tyrosines in transmembrane segment 11.Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein.Multidrug resistance protein 4 (ABCC4)-mediated ATP hydrolysis: effect of transport substrates and characterization of the post-hydrolysis transition state.The topography of transmembrane segment six is altered during the catalytic cycle of P-glycoprotein.Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane.Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site.Introduction of the most common cystic fibrosis mutation (Delta F508) into human P-glycoprotein disrupts packing of the transmembrane segments.Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR).Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein.The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence.P-glycoprotein catalytic mechanism: studies of the ADP-vanadate inhibited state.Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein.Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein.
P2860
Q21145873-95A61862-BC87-4520-9B70-F044BE7EEB40Q24676413-FAC93C56-CD4B-4049-A54E-88D136DA04DBQ33185124-748E0CFC-7EA5-4DFC-A286-CE5148E36E3AQ33193592-5FD2DD90-7536-4BE5-B774-35C7F498F03DQ33401731-9D542420-B442-4FEC-9531-178C9A31D19AQ35294152-A1EAE508-0B09-47F3-BA11-2EF0BB6D31A2Q35644350-6976AF6B-AFA2-4D1F-A0DA-D78774E3AE26Q36137412-10E26975-5EDE-46BC-A0FF-CB1D1077CD04Q36354417-24B37793-3539-478F-812A-9D3D53DF5C76Q36525551-D65C161E-2118-4566-8867-00FE2D395D29Q36876759-187A09A3-2D74-41F0-A603-EAE56752FC62Q37355834-7F0C58A1-052A-4582-B548-5553A76348DDQ37653308-09CD1846-9433-4433-AB7A-23907445FB88Q38341900-3EF3A790-9279-4905-85A4-D85887B7737FQ39341118-BA122A06-E63B-4BF7-976E-DC2BEA323288Q39828462-B88C9A73-07D6-4DDF-844A-CA8D1066AC65Q39966104-237CFB8D-3662-4139-BFE6-2010DC0CAFBAQ40310701-F04DF363-3C1C-4A6C-8612-20E82C6B27B0Q40516141-D7FFE46E-658F-466E-AA23-5EEDEB3445C7Q40546719-8032587B-6FCA-4554-B58C-55ECD716492BQ40608295-4AF3015E-21A3-4BB7-9785-AA53C4EBA062Q40652649-BB911E17-CF8F-49F1-B10C-2598C884BAC3Q40724271-395D987B-EE28-42BA-94AD-79B702C4E390Q41993227-50C578AD-9F9D-4203-AB6E-0A62CC3493A7Q42451287-CA95E505-B1E1-4F46-B2FB-37DCAAAA6E77Q44133854-EAC14D99-DD49-4F38-B252-AB2D8529F5BAQ44387458-0A900AA1-C7CE-4CA5-8161-774D7FB6FDC2Q44543802-D3A5BF5E-BF21-4844-87D2-CEF1E58C9783Q44746508-80854837-8866-4AB8-95E4-BABBCCD9113C
P2860
Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site
description
2002 nî lūn-bûn
@nan
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@ast
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@en
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@nl
type
label
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@ast
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@en
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@nl
prefLabel
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@ast
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@en
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@nl
P2860
P356
P1476
Vanadate trapping of nucleotid ...... idues to the drug-binding site
@en
P2093
David M Clarke
P2860
P304
P356
10.1073/PNAS.022049799
P407
P50
P577
2002-03-12T00:00:00Z