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Int. J. Mol. Sci. 2010, 11(4), 1808-1824; doi:10.3390/ijms11041808
Review

Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

1, 2 and 1,*
1 Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville 3052, Australia 2 Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand
* Author to whom correspondence should be addressed.
Received: 1 March 2010 / Revised: 23 March 2010 / Accepted: 14 April 2010 / Published: 16 April 2010
(This article belongs to the Special Issue Advances in Molecular Recognition)
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Abstract

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.
Keywords: apoptosis; Bcl-2; BH3-only; intrinsically disordered protein; protein structure apoptosis; Bcl-2; BH3-only; intrinsically disordered protein; protein structure
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Rautureau, G.J.P.; Day, C.L.; Hinds, M.G. Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis. Int. J. Mol. Sci. 2010, 11, 1808-1824.

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