ArticleScientific reports2016
Changes in the folding landscape of the WW domain provide a molecular mechanism for an inherited genetic syndrome.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Renpenning syndrome caused by the c.459_462delAGAG mutation in PQBP1: a case report and literature review.Frontiers in genetics · 2026Article
- PQBP1: The Key to Intellectual Disability, Neurodegenerative Diseases, and Innate Immunity.International journal of molecular sciences · 2022Review
- The CSY-protecting group in the microwave-assisted synthesis of aggregation-prone peptides.RSC chemical biology · 2022Article
- Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation.Nature communications · 2021Article
- Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability.International journal of molecular sciences · 2021Review
- MotifAnalyzer-PDZ: A computational program to investigate the evolution of PDZ-binding target specificity.Protein science : a publication of the Protein Society · 2019Article
- Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Simple MD-based model for oxidative folding of peptides and proteins.Scientific reports · 2017Article
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
Abstract
WW domains are small domains present in many human proteins with a wide array of functions and acting through the recognition of proline-rich sequences. The WW domain belonging to polyglutamine tract-binding protein 1 (PQBP1) is of particular interest due to its direct involvement in several X chromosome-linked intellectual disabilities, including Golabi-Ito-Hall (GIH) syndrome, where a single point mutation (Y65C) correlates with the development of the disease. The mutant cannot bind to its natural ligand WBP11, which regulates mRNA processing. In this work we use high-field high-resolution NMR and enhanced sampling molecular dynamics simulations to gain insight into the molecular causes the disease. We find that the wild type protein is partially unfolded exchanging among multiple beta-strand-like conformations in solution. The Y65C mutation further destabilizes the residual fold and primes the protein for the formation of a disulphide bridge, which could be at the origin of the loss of function.
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Registered trials
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