- SASDED2: Polyglutamine tract-binding protein 1 (PQBP-1) (Polyglutamine-bin... -
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基本情報
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データベース: SASBDB / ID: SASDED2
試料
Polyglutamine tract-binding protein 1 (PQBP-1)
Polyglutamine-binding protein 1 (protein), PQBP-1, Homo sapiens
機能・相同性
機能・相同性情報
neuronal ribonucleoprotein granule / alternative mRNA splicing, via spliceosome / regulation of dendrite morphogenesis / cellular response to exogenous dsRNA / regulation of RNA splicing / positive regulation of type I interferon production / ribonucleoprotein complex binding / positive regulation of defense response to virus by host / activation of innate immune response / mRNA Splicing - Major Pathway ...neuronal ribonucleoprotein granule / alternative mRNA splicing, via spliceosome / regulation of dendrite morphogenesis / cellular response to exogenous dsRNA / regulation of RNA splicing / positive regulation of type I interferon production / ribonucleoprotein complex binding / positive regulation of defense response to virus by host / activation of innate immune response / mRNA Splicing - Major Pathway / cytoplasmic stress granule / neuron projection development / double-stranded DNA binding / defense response to virus / transcription coactivator activity / nuclear body / nuclear speck / innate immune response / regulation of DNA-templated transcription / DNA binding / nucleoplasm / nucleus / cytoplasm 類似検索 - 分子機能
ジャーナル: Biophys J / 年: 2012 タイトル: Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. 著者: Martin Rees / Christian Gorba / Cesira de Chiara / Tam T T Bui / Mitla Garcia-Maya / Alex F Drake / Hitoshi Okazawa / Annalisa Pastore / Dmitri Svergun / Yu Wai Chen / 要旨: 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 ...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.