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Nucleic Acids Res. 2011 Jan;39(Database issue):D272-6. doi: 10.1093/nar/gkq1100. Epub 2010 Nov 8.

PolyQ: a database describing the sequence and domain context of polyglutamine repeats in proteins.

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1
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Nursing and Health Sciences, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.

Abstract

The polyglutamine diseases are caused in part by a gain-of-function mechanism of neuronal toxicity involving protein conformational changes that result in the formation and deposition of β-sheet rich aggregates. Recent evidence suggests that the misfolding mechanism is context-dependent, and that properties of the host protein, including the domain architecture and location of the repeat tract, can modulate aggregation. In order to allow the bioinformatic investigation of the context of polyglutamines, we have constructed a database, PolyQ (http://pxgrid.med.monash.edu.au/polyq). We have collected the sequences of all human proteins containing runs of seven or more glutamine residues and annotated their sequences with domain information. PolyQ can be interrogated such that the sequence context of polyglutamine repeats in disease and non-disease associated proteins can be investigated.

PMID:
21059684
PMCID:
PMC3013692
DOI:
10.1093/nar/gkq1100
[Indexed for MEDLINE]
Free PMC Article
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