Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
- Author(s)
- Rautureau, GJP; Day, CL; Hinds, MG;
- Details
- Publication Year 2010-04,Volume 11,Issue #4,Page 1808-1824
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Publication Type
- Journal Article
- Abstract
- 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.
- Publisher
- MDPI AG
- Keywords
- CELL-DEATH MACHINERY; DYNEIN LIGHT-CHAIN; BH3-ONLY PROTEINS; FAMILY-MEMBERS; MITOCHONDRIAL-MEMBRANE; UNSTRUCTURED PROTEINS; SIGNALING PATHWAY; CRYSTAL-STRUCTURE; INDUCE APOPTOSIS; STRUCTURAL BASIS
- Publisher's Version
- https://doi.org/10.3390/ijms11041808
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2010-04-01 12:00:00