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

Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD.

Nature communications - 30 Apr 2014

Mizuguchi Mineyuki, Obita Takayuki, Serita Tomohito, Kojima Rieko, Nabeshima Yuko, Okazawa Hitoshi

Abstract excerpt

A loss-of-function of polyglutamine tract-binding protein 1 (PQBP1) induced by frameshift mutations is believed to cause X-linked mental retardation. However, the mechanism by which structural changes in PQBP1 lead to mental retardation is unknown. Here we present the crystal structure of a C-terminal fragment of PQBP1 in complex with the spliceosomal protein U5-15 kD. The U5-15 kD hydrophobic groove recognizes a...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Chromatography, Gel

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

Share to Crystallization

Share to Fluorescence

Share to Magnetic Resonance Spectroscopy

Share to Protein Conformation

Share to Ribonucleoprotein, U5 Small Nuclear

Share to Spliceosomes

Source

Identifiers

PMID: 24781215
DOI: 10.1038/ncomms4822

Genes

PQBP1

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

Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD.PMID 24781215Read ↗

[Frameshift mutations in the PQBP1 gene prevent its interaction with the splicing factor U5-15kD].Semantic proximity Read ↗

[Structural study of polyglutamine tract-binding protein 1].Semantic proximity Read ↗

Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing.Semantic proximity Read ↗

Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1.Semantic proximity Read ↗

Common pathological mutations in PQBP1 induce nonsense-mediated mRNA decay and enhance exclusion of the mutant exon.Semantic proximity Read ↗

A mild clinical and neuropsychological phenotype of Renpenning syndrome: A new case report with a maternally inherited PQBP1 missense mutation.Semantic proximity Read ↗

Mutations in the polyglutamine binding protein 1 gene cause X-linked mental retardation.Semantic proximity Read ↗

Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Semantic proximity Read ↗

Molecular mechanism for the interaction between human CPSF30 and hFip1.Semantic proximity Read ↗

Genotype-phenotype studies in three families with mutations in the polyglutamine-binding protein 1 gene (PQBP1).Semantic proximity Read ↗

Protein-protein and protein-RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs.Semantic proximity Read ↗

Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.Semantic proximity Read ↗

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