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• W2023269957 abstract "Mutations or deletions of FMRP, involved in the regulation of mRNA metabolism in brain, lead to the Fragile X syndrome (FXS), the most frequent form of inherited intellectual disability. A severe manifestation of the disease has been associated with the Ile304Asn mutation, located on the KH2 domain of the protein. Several hypotheses have been proposed to explain the possible molecular mechanism responsible for the drastic effect of this mutation in humans. Here, we performed a molecular dynamics simulation and show that the Ile304Asn mutation destabilizes the hydrophobic core producing a partial unfolding of two α-helices and a displacement of a third one. The affected regions show increased residue flexibility and motion. Molecular docking analysis revealed strongly reduced binding to a model single-stranded nucleic acid in agreement with known data that the two partially unfolded helices form the RNA-binding surface. The third helix, which we show here to be also affected, is involved in the PAK1 protein interaction. These two functional binding sites on the KH2 domain do not overlap spatially, and therefore, they can simultaneously bind their targets. Since the Ile304Asn mutation affects both binding sites, this may justify the severe clinical manifestation observed in the patient in which both mRNA metabolism activity and cytoskeleton remodeling would be affected." @default.
• W2023269957 created "2016-06-24" @default.
• W2023269957 creator A5017201543 @default.
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• W2023269957 creator A5079658433 @default.
• W2023269957 creator A5086204590 @default.
• W2023269957 date "2013-03-25" @default.
• W2023269957 modified "2023-10-16" @default.
• W2023269957 title "Molecular dynamics simulations show how the FMRP Ile304Asn mutation destabilizes the KH2 domain structure and affects its function" @default.
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• W2023269957 doi "https://doi.org/10.1080/07391102.2013.768552" @default.
• W2023269957 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23527791" @default.
• W2023269957 hasPublicationYear "2013" @default.
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