Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Involvement of the "occluded nucleotide conformation" of P-glycoprotein in the catalytic pathway.

Biochemistry - 27 Sept 2005

Tombline Gregory, Muharemagić Alma, White Lori Bartholomew, Senior Alan E

Abstract excerpt

We found recently that the combined mutation of both "catalytic carboxylate" residues (E552A/E1197A) in mouse P-glycoprotein (Pgp) arrested the protein in an "occluded nucleotide conformation", possibly a stabilized dimer of nucleotide-binding domains (NBDs), that binds MgATP tightly at stoichiometry of 1 mol/mol Pgp [Tombline, G., Bartholomew, L., Urbatsch, I. L., and Senior, A. E. (2004) J. Biol. Chem. 279,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to ATP Binding Cassette Transporter, Subfamily B, Member 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Azides

Share to Catalysis

Share to Enzyme Inhibitors

Share to Ethylmaleimide

Share to Glutamic Acid

Share to Verapamil

Source

Identifiers

PMID: 16171403
DOI: 10.1021/bi0509797

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Involvement of the "occluded nucleotide conformation" of P-glycoprotein in the catalytic pathway.PMID 16171403Read ↗

Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues.Semantic proximity Read ↗

Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity.Semantic proximity Read ↗

Binding of ATP at the active site of human pancreatic glucokinase--nucleotide-induced conformational changes with possible implications for its kinetic cooperativity.Semantic proximity Read ↗

Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer-associated P-glycoprotein during ATP hydrolysis.Semantic proximity Read ↗

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation.Semantic proximity Read ↗

Nucleotide-induced Structural Changes in P-glycoprotein Observed by Electron MicroscopySemantic proximity Read ↗

On the mechanism of MgATP-dependent gating of CFTR Cl- channels.Semantic proximity Read ↗

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism.Semantic proximity Read ↗

Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy.Semantic proximity Read ↗

Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase.Semantic proximity Read ↗

Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.Semantic proximity Read ↗

Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.