The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.
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Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transportersThe ABC protein turned chloride channel whose failure causes cystic fibrosisCFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).Peroxisomal ABC transporters: functions and mechanismStructures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutantATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerizationDevelopment of CFTR StructureATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.Mutational analysis of Cvab, an ABC transporter involved in the secretion of active colicin V.CFTR and TNR-CFTR expression and function in the kidney.Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter.Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.ATP-independent CFTR channel gating and allosteric modulation by phosphorylation.Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channelADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.A survey of detergents for the purification of stable, active human cystic fibrosis transmembrane conductance regulator (CFTR).Structure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects.A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening.Sequences in the nonconsensus nucleotide-binding domain of ABCG5/ABCG8 required for sterol transportMutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingCysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Structure and function of efflux pumps that confer resistance to drugsRegulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.ATP-sensitive K+ channel channel/enzyme multimer: metabolic gating in the heart.Molecular modelling and molecular dynamics of CFTR.Adenylate kinase activity in ABC transporters.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Demonstration of phosphoryl group transfer indicates that the ATP-binding cassette (ABC) transporter cystic fibrosis transmembrane conductance regulator (CFTR) exhibits adenylate kinase activityInsight in eukaryotic ABC transporter function by mutation analysis.On the mechanism of MgATP-dependent gating of CFTR Cl- channelsFunctional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain.Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.Distinct Mg(2+)-dependent steps rate limit opening and closing of a single CFTR Cl(-) channel.Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.Role for SUR2A ED domain in allosteric coupling within the K(ATP) channel complex.
P2860
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P2860
The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.
description
2002 nî lūn-bûn
@nan
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
2002年论文
@zh
2002年论文
@zh-cn
name
The First Nucleotide Binding D ...... d Is a Site of Rapid Turnover.
@en
type
label
The First Nucleotide Binding D ...... d Is a Site of Rapid Turnover.
@en
prefLabel
The First Nucleotide Binding D ...... d Is a Site of Rapid Turnover.
@en
P2093
P2860
P356
P1476
The First Nucleotide Binding D ...... d Is a Site of Rapid Turnover.
@en
P2093
Andrei A Aleksandrov
John R Riordan
Luba Aleksandrov
Xiu-Bao Chang
P2860
P304
15419-15425
P356
10.1074/JBC.M111713200
P407
P577
2002-02-22T00:00:00Z