A computational analysis of S -(2-succino)cysteine sites in proteins
作者: Gianluca MiglioAlessandro Damiano SabatinoEleonora VegliaMaria Teresa GiraudoMarco BeccutiFrancesca Cordero
作者单位: 1Dipartimento di Scienza e Tecnologia del Farmaco, Università degli Studi di Torino, Turin, Italy
2Department of Mathematics and Statistics, University of Strathclyde, Glasgow, UK
3Dipartimento di Matematica “Giuseppe Peano”, Università degli Studi di Torino, Turin, Italy
4Dipartimento di Informatica, Università degli Studi di Torino, Turin, Italy
刊名: BBA - Proteins and Proteomics, 2016, Vol.1864 (2), pp.211-218
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbapap.2015.11.003
关键词: Protein succinationS -(2-succino)cysteine sitesCysteine reactivityFumaric acid
原始语种摘要: Abstract(#br)The adduction of fumaric acid to the sulfhydryl group of certain cysteine (Cys) residues in proteins via a Michael-like reaction leads to the formation of S -(2-succino)cysteine (2SC) sites. Although its role remains to be fully understood, this post-translational Cys modification (protein succination) has been implicated in the pathogenesis of diabetes/obesity and fumarate hydratase-related diseases. In this study, theoretical approaches to address sequence- and 3D-structure-based features possibly underlying the specificity of protein succination have been applied to perform the first analysis of the available data on the succinate proteome . A total of 182 succinated proteins, 205 modifiable, and 1750 non-modifiable sites have been examined. The rate of 2SC sites per...
全文获取路径: Elsevier  (合作)
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