Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter - Wikidata - awgldk - TriplyDB

Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter

Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter

http://www.wikidata.org/entity/Q34377172

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Crystal structure of the maltose transporter in a pretranslocation intermediate state Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domain The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding Domains Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy Two-photon excited UV fluorescence for protein crystal detection Structural diversity of ABC transporters.An asymmetric post-hydrolysis state of the ABC transporter ATPase dimer.Molecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state Structural characterization of two metastable ATP-bound states of P-glycoprotein.Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle.Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy.D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter Mechanism of the ABC transporter ATPase domains: catalytic models and the biochemical and biophysical record.Molecular mechanism of the Escherichia coli maltose transporter.Allosteric transitions of the maltose transporter studied by an elastic network model.Nucleotide-free MalK drives the transition of the maltose transporter to the inward-facing conformation.Nanodiscs in Membrane Biochemistry and Biophysics.Conformational cycle of the vitamin B12 ABC importer in liposomes detected by double electron-electron resonance (DEER).Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin Transporter Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2.From substrate specificity to promiscuity: hybrid ABC transporters for osmoprotectants.Substrate versus inhibitor dynamics of P-glycoprotein.Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK2 and Catalytic Roles of ATP, MalE, and Maltose.Allosteric effects of ATP binding on the nucleotide-binding domain of a heterodimeric ATP-binding cassette transporter.Coupling between ATP hydrolysis and protein conformational change in maltose transporter.Conformational dynamics in binding-protein-independent mutant of the Escherichia coli maltose transporter, MalG511 and its interaction with maltose binding protein.Targeting Nucleotide Binding Domain of Multidrug Resistance-associated Protein-1 (MRP1) for the Reversal of Multi Drug Resistance in Cancer

P2860

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P2860

Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter

http://www.wikidata.org/entity/Q34377172

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

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name

Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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type

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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Dynamics of alpha-helical subd ...... P-binding cassette transporter

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PNAS.1006544107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Dynamics of alpha-helical subd ...... P-binding cassette transporter

@en

P2093

Amy L Davidson

http://www.w3.org/2001/XMLSchema#string

Cédric Orelle

http://www.w3.org/2001/XMLSchema#string

Frances Joan D Alvarez

http://www.w3.org/2001/XMLSchema#string

Jue Chen

http://www.w3.org/2001/XMLSchema#string

Michael L Oldham

http://www.w3.org/2001/XMLSchema#string

Theodore E Wiley

http://www.w3.org/2001/XMLSchema#string

P2860

Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

ABC transporters: the power to change

Structural insights into ABC transporter mechanism

Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding

Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains

A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle

Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP

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20293-20298

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10.1073/PNAS.1006544107

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47

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107

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2010-11-08T00:00:00Z

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47717896

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21059948

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2996640

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