ArticleThe Journal of biological chemistry2014
Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Abnormal Splicing in the Final Intron of PRX Results in Dominant Congenital Cataract Without Neurological Phenotype.Investigative ophthalmology & visual science · 2025Article
- Periaxin gene variants are linked to age-related cataracts in Cx46 deficient lenses.Communications biology · 2025Article
- AHNAKs roles in physiology and malignant tumors.Frontiers in oncology · 2023Review
- AHNAK Contributes to Hepatocellular Carcinoma Growth by Interacting with IGF-1R.Molecules (Basel, Switzerland) · 2022Article
- Exome sequencing in a child with neurodevelopmental disorder and epilepsy: Variant analysis of the AHNAK2 gene.Molecular genetics & genomic medicine · 2022Article
- AHNAK2 is a biomarker and a potential therapeutic target of adenocarcinomas.Acta biochimica et biophysica Sinica · 2022Article
- Ahnak depletion accelerates liver regeneration by modulating the TGF-β/Smad signaling pathway.BMB reports · 2022Article
- The Obscure Potential of AHNAK2.Cancers · 2022Review
- Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.PloS one · 2021Article
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- AHNAK2 Is Associated with Poor Prognosis and Cell Migration in Lung Adenocarcinoma.BioMed research international · 2020Article
- Linkage analysis and whole exome sequencing reveals AHNAK2 as a novel genetic cause for autosomal recessive CMT in a Malaysian family.Neurogenetics · 2019Article
- Direct Binding of the Flexible C-Terminal Segment of Periaxin to β4 Integrin Suggests a Molecular Basis for CMT4F.Frontiers in molecular neuroscience · 2019Article
- Melanoma Tumor Characteristics: An Analysis of Mutational Burden and Copy Number Alterations by Patient Age and Stage.The Journal of investigative dermatology · 2018Article
- AHNAK suppresses tumour proliferation and invasion by targeting multiple pathways in triple-negative breast cancer.Journal of experimental & clinical cancer research : CR · 2017Article
- Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin.Data in brief · 2017Article
- Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.Protein science : a publication of the Protein Society · 2017Article
- Intermolecular disulfide bond in the dimerization of S-periaxin mediated by Cys88 and Cys139.Acta biochimica et biophysica Sinica · 2016Article
- Two independently folding units of Plasmodium profilin suggest evolution via gene fusion.Cellular and molecular life sciences : CMLS · 2015Article
- Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping.Protein science : a publication of the Protein Society · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Periaxin (PRX) is an abundant protein in the peripheral nervous system, with an important role in myelination. PRX participates in large molecular complexes, most likely through the interactions of its N-terminal PSD-95/Discs-large/ZO-1 (PDZ)-like domain. We present the crystal structures of the PDZ-like domains from PRX and its homologue AHNAK nucleoprotein 2 (AHNAK2). The unique intertwined, domain-swapped dimers provide a structural basis for the homodimerization of both proteins. The core of the homodimer is formed by a 6-stranded antiparallel β sheet, with every other strand from a different chain. The AHNAK2 PDZ domain structure contains a bound class III ligand peptide. The binding pocket is preformed, and the peptide-PDZ interactions have unique aspects, including two salt bridges and weak recognition of the peptide C terminus. Tight homodimerization may be central to the scaffolding functions of PRX and AHNAK2 in molecular complexes linking the extracellular matrix to the cytoskeletal network.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.