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

Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations.

Proceedings of the National Academy of Sciences of the United States of America - 4 Apr 2006

Dmitriev Oleg, Tsivkovskii Ruslan, Abildgaard Frits, Morgan Clinton T, Markley John L, Lutsenko Svetlana

Abstract excerpt

Wilson disease protein (ATP7B) is a copper-transporting P(1B)-type ATPase that regulates copper homeostasis and biosynthesis of copper-containing enzymes in human tissues. Inactivation of ATP7B or related ATP7A leads to severe neurodegenerative disorders, whereas their overexpression contributes to cancer cell resistance to chemotherapeutics. Copper-transporting ATPases differ from other P-type ATPases in their...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Binding Sites

Share to Cation Transport Proteins

Share to Copper-Transporting ATPases

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 16567646
DOI: 10.1073/pnas.0507416103
PMCID: PMC1459350

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations.PMID 16567646Read ↗

The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F.Semantic proximity Read ↗

Stability and ATP binding of the nucleotide-binding domain of the Wilson disease protein: effect of the common H1069Q mutation.Semantic proximity Read ↗

The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.Semantic proximity Read ↗

A structural model of the copper ATPase ATP7B to facilitate analysis of Wilson disease-causing mutations and studies of the transport mechanism.Semantic proximity Read ↗

Sequence variation in the ATP-binding domain of the Wilson disease transporter, ATP7B, affects copper transport in a yeast model system.Semantic proximity Read ↗

The Structure of Metal Binding Domain 1 of the Copper Transporter ATP7B Reveals Mechanism of a Singular Wilson Disease MutationSemantic proximity Read ↗

Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations.Semantic proximity Read ↗

Sequence variation database for the Wilson disease copper transporter, ATP7B.Semantic proximity Read ↗

Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation.Semantic proximity Read ↗

Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B.Semantic proximity Read ↗

Characterization of mutation spectrum and identification of novel mutations in ATP7B gene from a cohort of Wilson disease patients: Functional and therapeutic implications.Semantic proximity Read ↗

Analysis of Wilson disease mutations revealed that interactions between different ATP7B mutants modify their properties.Semantic proximity Read ↗

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