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

Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

1, 2 and 1,* email
Received: 1 March 2010; in revised form: 23 March 2010 / Accepted: 14 April 2010 / Published: 16 April 2010
(This article belongs to the Special Issue Advances in Molecular Recognition)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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
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MDPI and ACS Style

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.

AMA Style

Rautureau GJP, Day CL, Hinds MG. Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis. International Journal of Molecular Sciences. 2010; 11(4):1808-1824.

Chicago/Turabian Style

Rautureau, Gilles J. P.; Day, Catherine L.; Hinds, Mark G. 2010. "Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis." Int. J. Mol. Sci. 11, no. 4: 1808-1824.

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