Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival 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 splic...

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Main Authors: Gilles J. P. Rautureau, Catherine L. Day, Mark G. Hinds
Format: Article
Language:English
Published: MDPI AG 2010-04-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:http://www.mdpi.com/1422-0067/11/4/1808/
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author Gilles J. P. Rautureau
Catherine L. Day
Mark G. Hinds
author_facet Gilles J. P. Rautureau
Catherine L. Day
Mark G. Hinds
author_sort Gilles J. P. Rautureau
collection DOAJ
description Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival 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.
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spelling doaj.art-8c067c8d2568476d815a25ea1aa0e7b22022-12-22T03:29:30ZengMDPI AGInternational Journal of Molecular Sciences1422-00672010-04-011141808182410.3390/ijms11041808Intrinsically Disordered Proteins in Bcl-2 Regulated ApoptosisGilles J. P. RautureauCatherine L. DayMark G. HindsIntrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival 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.http://www.mdpi.com/1422-0067/11/4/1808/apoptosisBcl-2BH3-onlyintrinsically disordered proteinprotein structure
spellingShingle Gilles J. P. Rautureau
Catherine L. Day
Mark G. Hinds
Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
International Journal of Molecular Sciences
apoptosis
Bcl-2
BH3-only
intrinsically disordered protein
protein structure
title Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_full Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_fullStr Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_full_unstemmed Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_short Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_sort intrinsically disordered proteins in bcl 2 regulated apoptosis
topic apoptosis
Bcl-2
BH3-only
intrinsically disordered protein
protein structure
url http://www.mdpi.com/1422-0067/11/4/1808/
work_keys_str_mv AT gillesjprautureau intrinsicallydisorderedproteinsinbcl2regulatedapoptosis
AT catherinelday intrinsicallydisorderedproteinsinbcl2regulatedapoptosis
AT markghinds intrinsicallydisorderedproteinsinbcl2regulatedapoptosis