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Biochim Biophys Acta. 2009 Jun;1794(6):936-43. doi: 10.1016/j.bbapap.2009.03.001. Epub 2009 Mar 17.

Polyglutamine tract binding protein-1 is an intrinsically unstructured protein.

Author information

1
Faculty of Pharmaceutical Sciences, University of Toyama, 2630, Sugitani, Toyama 930-0194, Japan.

Abstract

Polyglutamine tract binding protein-1 (PQBP-1) is a nuclear protein that interacts with disease proteins containing expanded polyglutamine repeats. PQBP-1 also interacts with RNA polymerase II and a spliceosomal protein U5-15kD. In the present study, we demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. Intriguingly, the large unstructured region encompasses two functional domains: a polar amino acid rich domain and a C-terminal domain. These findings suggest that PQBP-1 belongs to the family of intrinsically unstructured/disordered proteins. Furthermore, the binding of the target molecule U5-15kD induces only minor conformational changes into PQBP-1. Our results suggest that PQBP-1 includes high content of unstructured regions in the C-terminal domain, in spite of the binding of U5-15kD.

PMID:
19303059
DOI:
10.1016/j.bbapap.2009.03.001
[Indexed for MEDLINE]

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