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- W2000399543 abstract "Polyglutamine tract-binding protein-1 (PQBP-1) is a 265-residue nuclear protein that is involved in transcriptional regulation. In addition to its role in the molecular pathology of the polyglutamine expansion diseases, mutations of the protein are associated with X-linked mental retardation. PQBP-1 binds specifically to glutamine repeat sequences and proline-rich regions, and interacts with RNA polymerase II and the spliceosomal protein U5-15kD. In this work, we obtained a biophysical characterization of this protein by employing complementary structural methods. PQBP-1 is shown to be a moderately compact but largely disordered molecule with an elongated shape, having a Stokes radius of 3.7 nm and a maximum molecular dimension of 13 nm. The protein is monomeric in solution, has residual β-structure, and is in a premolten globule state that is unaffected by natural osmolytes. Using small-angle x-ray scattering data, we were able to generate a low-resolution, three-dimensional model of PQBP-1." @default.
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- W2000399543 date "2012-04-01" @default.
- W2000399543 modified "2023-10-18" @default.
- W2000399543 title "Solution Model of the Intrinsically Disordered Polyglutamine Tract-Binding Protein-1" @default.
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- W2000399543 doi "https://doi.org/10.1016/j.bpj.2012.02.047" @default.
- W2000399543 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3318138" @default.
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