(PDF) Combined Mutation of Catalytic Glutamate Residues in

Combined Mutation of Catalytic Glutamate Residues in the Two Nucleotide Binding Domains of P-Glycoprotein Generates a Conformation That Binds ATP and ADP Tightly

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m404689200

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May 24, 2004

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American Society for Biochemistry & Molecular Biology (ASBMB)

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Combined Mutation of Catalytic Glutamate Residues in the Two Nucleotide Binding Domains of P-Glycoprotein Generates a Conformation That Binds ATP and ADP Tightly

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m404689200

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

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

Spectroscopic Studies of the Dimerization of ATP-Binding Cassette Nucleotide-Binding Domains

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

Conformational Changes of P-Glycoprotein by Nucleotide Binding

Processing Mutations Located Throughout the Human Multidrug Resistance P-Glycoprotein Disrupt Interactions Between the Nucleotide Binding Domains

The Transmembrane Prolines of the Mitochondrial ADP/ATP Carrier Are Involved in Nucleotide Binding and Transport and Its Biogenesis

Curcumin Opens Cystic Fibrosis Transmembrane Conductance Regulator Channels by a Novel Mechanism That Requires Neither ATP Binding Nor Dimerization of the Nucleotide-Binding Domains

Three-Dimensional Structures of the Mammalian Multidrug Resistance P-Glycoprotein Demonstrate Major Conformational Changes in the Transmembrane Domains Upon Nucleotide Binding

Lipid Binding and Lipid-Uptake in P-Glycoprotein: Comparison of the Inward- And Outward-Facing Conformation