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

Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1.

The Journal of biological chemistry - 7 Jul 2000

Hou Y, Cui L, Riordan J R, Chang X

Abstract excerpt

Membrane transporters of the adenine nucleotide binding cassette (ABC) superfamily utilize two either identical or homologous nucleotide binding domains (NBDs). Although the hydrolysis of ATP by these domains is believed to drive transport of solute, it is unknown why two rather than a single NBD is required. In the well studied P-glycoprotein multidrug transporter, the two appear to be functionally equivalent,...

Read the complete abstract on PubMed

Topics

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

Share to Adenine Nucleotides
Share to Adenosine Diphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Adenosine Triphosphate

Share to Allosteric Regulation

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

Share to ATP-Binding Cassette Transporters

Share to Azides

Share to Doxorubicin

Source

Identifiers

PMID: 10781583
DOI: 10.1074/jbc.M001109200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1.PMID 10781583Read ↗

ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.Semantic proximity Read ↗

Nonequivalent Nucleotide Trapping in the Two Nucleotide Binding Folds of the Human Multidrug Resistance Protein MRP1Semantic proximity Read ↗

A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1Semantic proximity Read ↗

Function of the ABC signature sequences in the human multidrug resistance protein 1.Semantic proximity Read ↗

Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1.Semantic proximity Read ↗

Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1).Semantic proximity Read ↗

Analysis of the properties of the N-terminal nucleotide-binding domain of human P-glycoprotein.Semantic proximity Read ↗

Conserved amino acids in the region connecting membrane spanning domain 1 to nucleotide binding domain 1 are essential for expression of the MRP1 (ABCC1) transporter.Semantic proximity Read ↗

Effect of Walker A mutation (K86M) on oligomerization and surface targeting of the multidrug resistance transporter ABCG2.Semantic proximity Read ↗

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

The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers.Semantic proximity Read ↗

Interaction of the nucleotide binding domains and regulation of the ATPase activity of the human retina specific ABC transporter, ABCR.Semantic proximity Read ↗

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