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Solution Model of the Intrinsically Disordered Polyglutamine Tract-Binding Protein-1
DOI:
10.1016/j.bpj.2012.02.047
Authors:
Martin
Rees
(King's College London)
,
Christian
Gorba
(European Molecular Biology Laboratory)
,
Cesira
De chiara
(Medical Research Council National Institute of Medical Research)
,
Tam t.t.
Bui
(King's College London)
,
Mitla
Garcia-maya
(King's College London)
,
Alex f.
Drake
(King's College London)
,
Hitoshi
Okazawa
(Tokyo Medical and Dental University)
,
Annalisa
Pastore
(Medical Research Council National Institute of Medical Research)
,
Dmitri
Svergun
(European Molecular Biology Laboratory)
,
Yu Wai
Chen
(King's College London)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Biophysical Journal
, VOL 102 (7)
, PAGES 1608 - 1616
State:
Published (Approved)
Published:
April 2012
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 ?-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.
Subject Areas:
Biology and Bio-materials,
Physics,
Medicine
Instruments:
B23-Circular Dichroism
Other Facilities: DESY
Added On:
02/04/2013 12:53
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