Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

被引：59

作者：

Rautureau, Gilles J. P. ^{[1
]}

Day, Catherine L. ^{[2
]}

Hinds, Mark G. ^{[1
]}

机构：

[1] Walter & Eliza Hall Inst Med Res, Parkville, Vic 3052, Australia

[2] Univ Otago, Dept Biochem, Dunedin 9054, New Zealand

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2010年 / 11卷 / 04期

关键词：

apoptosis; Bcl-2; BH3-only; intrinsically disordered protein; protein structure; CELL-DEATH MACHINERY; DYNEIN LIGHT-CHAIN; BH3-ONLY PROTEINS; FAMILY-MEMBERS; MITOCHONDRIAL-MEMBRANE; UNSTRUCTURED PROTEINS; SIGNALING PATHWAY; CRYSTAL-STRUCTURE; INDUCE APOPTOSIS; STRUCTURAL BASIS;

D O I：

10.3390/ijms11041808

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Intrinsic cell death is mediated by interaction between pro-apoptotic and prosurvival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splicing and post-translational modifications can determine the extent of these disordered regions and are critical for regulating Bcl-2 proteins. Conformational plasticity and structural transitions characterize the interactions within the Bcl-2 family, with conserved sequence motifs on both binding partners required for their molecular recognition.

引用

页码：1808 / 1824

页数：17

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