Robertson Amy L, Bate Mark A, Androulakis Steve G, Bottomley Stephen P, Buckle Ashley M
Department of Biochemistry and Molecular Biology, Faculty of Medicine, Nursing and Health Sciences, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.
Nucleic Acids Res. 2011 Jan;39(Database issue):D272-6. doi: 10.1093/nar/gkq1100. Epub 2010 Nov 8.
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.
多聚谷氨酰胺疾病部分是由神经元毒性的功能获得机制引起的,该机制涉及蛋白质构象变化,导致富含β折叠的聚集体形成和沉积。最近的证据表明,错误折叠机制取决于环境,宿主蛋白的特性,包括结构域结构和重复序列的位置,可以调节聚集。为了对多聚谷氨酰胺的环境进行生物信息学研究,我们构建了一个数据库PolyQ(http://pxgrid.med.monash.edu.au/polyq)。我们收集了所有含有七个或更多谷氨酰胺残基连续序列的人类蛋白质的序列,并用结构域信息注释了它们的序列。可以查询PolyQ,以便研究疾病相关和非疾病相关蛋白质中多聚谷氨酰胺重复序列的序列环境。