The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating. - Wikidata - awgldk - TriplyDB

The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating.

The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating.

http://www.wikidata.org/entity/Q40315163

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Allosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTR The silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunction Genetic selection for a highly functional cysteine-less membrane protein using site saturation mutagenesis Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an alpha-helix.Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating Rational Coupled Dynamics Network Manipulation Rescues Disease-Relevant Mutant Cystic Fibrosis Transmembrane Conductance Regulator.Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.A stable human-cell system overexpressing cystic fibrosis transmembrane conductance regulator recombinant protein at the cell surface Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809.Some gating potentiators, including VX-770, diminish ΔF508-CFTR functional expression.Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activity Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator.Interaction between 2 extracellular loops influences the activity of the cystic fibrosis transmembrane conductance regulator chloride channel.Functional stability of rescued delta F508 cystic fibrosis transmembrane conductance regulator in airway epithelial cells.Role of the juxtamembrane region of cytoplasmic loop 3 in the gating and conductance of the cystic fibrosis transmembrane conductance regulator chloride channel.Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel.Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTR Cysteine-independent inhibition of the CFTR chloride channel by the cysteine-reactive reagent sodium (2-sulphonatoethyl) methanethiosulphonate.Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating.Using a cysteine-less mutant to provide insight into the structure and mechanism of CFTR.NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.Relationship between nucleotide binding and ion channel gating in cystic fibrosis transmembrane conductance regulator.A common mechanism for CFTR potentiators.Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant.Molecular dynamics simulation study on the structural instability of the most common cystic fibrosis-associated mutant ΔF508-CFTR.

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The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating.

http://www.wikidata.org/entity/Q40315163

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2006 nî lūn-bûn

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JPHYSIOL.2005.099457

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The Journal of Physiology

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The role of cystic fibrosis tr ...... e chain in ion channel gating.

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Andrei A Aleksandrov

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Jey-Hsin Chen

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John R Riordan

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Liying Cui

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Luba Aleksandrov

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Martina Gentzsch

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Yue-Xian Hou

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P2860

ATPase activity of the cystic fibrosis transmembrane conductance regulator

Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein

Effect of ATP concentration on CFTR Cl- channels: a kinetic analysis of channel regulation

Side chain and backbone contributions of Phe508 to CFTR folding.

The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR.

The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator.

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.

Differential interactions of nucleotides at the two nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator.

Rescue of dysfunctional deltaF508-CFTR chloride channel activity by IBMX.

Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis.

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10.1113/JPHYSIOL.2005.099457

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Pt 2

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572

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2006-02-16T00:00:00Z

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cystic fibrosis

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1779664

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