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

The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.

The Journal of general physiology - 1 Oct 2006

Zhou Zhen, Wang Xiaohui, Liu Hao-Yang, Zou Xiaoqin, Li Min, Hwang Tzyh-Chang

Abstract excerpt

Cystic fibrosis transmembrane conductance regulator (CFTR), a member of the ABC (ATP binding cassette) transporter family, is a chloride channel whose activity is controlled by protein kinase-dependent phosphorylation. Opening and closing (gating) of the phosphorylated CFTR is coupled to ATP binding and hydrolysis at CFTR's two nucleotide binding domains (NBD1 and NBD2). Recent studies present evidence that the...

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 CHO Cells

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cricetinae

Share to Cricetulus

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to Electrophysiology

Share to Ion Channel Gating

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 16966475
DOI: 10.1085/jgp.200609622
PMCID: PMC2151577

Genes

CFTR

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.PMID 16966475Read ↗

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.Semantic proximity Read ↗

Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.Semantic proximity Read ↗

A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.Semantic proximity Read ↗

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerizationSemantic proximity Read ↗

Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)Semantic proximity Read ↗

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation.Semantic proximity Read ↗

The most common cystic fibrosis‐associated mutation destabilizes the dimeric state of the nucleotide‐binding domains of CFTRSemantic proximity Read ↗

Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating.Semantic proximity Read ↗

Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle.Semantic proximity Read ↗

Nucleotide binding domains of human CFTR: a structural classification of critical residues and disease-causing mutations.Semantic proximity Read ↗

Timing of CFTR pore opening and structure of its transition state.Semantic proximity Read ↗

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