(PDF) A Stable ATP Binding to the Nucleotide Binding Domain

A Stable ATP Binding to the Nucleotide Binding Domain Is Important for Reliable Gating Cycle in an ABC Transporter CFTR

Journal of Physiological Sciences - Japan

doi 10.1007/s12576-010-0102-2

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July 14, 2010

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Springer Science and Business Media LLC

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Amanote Research

A Stable ATP Binding to the Nucleotide Binding Domain Is Important for Reliable Gating Cycle in an ABC Transporter CFTR

Journal of Physiological Sciences - Japan

doi 10.1007/s12576-010-0102-2

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Both Maltose-Binding Protein and ATP Are Required for Nucleotide-Binding Domain Closure in the Intact Maltose ABC Transporter

ATP Binding to Two Sites Is Necessary for Dimerization of Nucleotide-Binding Domains of ABC Proteins

Nucleotide-Dependent Conformational Changes in HisP: Molecular Dynamics Simulations of an ABC Transporter Nucleotide-Binding Domain

The Hydrolysis Cycle of ATP-Binding Cassette Nucleotide-Binding Domains

One Intact ATP-binding Subunit Is Sufficient to Support ATP Hydrolysis and Translocation in an ABC Transporter, the Histidine Permease

CFTR Gating Mechanism : The Role of Dimerization of Nucleotide Binding Domains

A Unified View of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Gating: Combining the Allosterism of a Ligand-Gated Channel With the Enzymatic Activity of an ATP-binding Cassette (ABC) Transporter

Transmembrane Gate Movements in the Type II ATP-binding Cassette (ABC) Importer BtuCD-F During Nucleotide Cycle

Nucleotide-Binding Domains of Cystic Fibrosis Transmembrane Conductance Regulator, an ABC Transporter, Catalyze Adenylate Kinase Activity but Not ATP Hydrolysis