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TitleSolution model of the intrinsically disordered polyglutamine tract-binding protein-1.
Journal, issue, pagesBiophys J, Vol. 102, Issue 7, Page 1608-1616, Year 2012
Publish dateApr 4, 2012
AuthorsMartin 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 /
PubMed AbstractPolyglutamine 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.
External linksBiophys J / PubMed:22500761 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDED2:
Polyglutamine tract-binding protein 1 (PQBP-1) (Polyglutamine-binding protein 1, PQBP-1)
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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