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Issue 1, 2012
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Dynamic optimization of signal transductionvia intrinsic disorder

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Abstract

It is widely accepted that the inherent flexibility of intrinsically disordered proteins (IDPs) correlates with essential functions in the cell such as signaling. However, the mechanisms by which disorder dynamically facilitates and optimizes signal transduction remain unclear. In this study, we have used a computational protocol to evaluate the interplay between the intrinsic disorder of p27kip1 and the collective motions of its binding partners, cyclin dependent kinase 2 (CDK2) and cyclin A (CA). We found that the synergy between intrinsic disorder of p27kip1 and the essential collective motions of the CDK2–CA complex introduces a set of sequential steps to dynamically optimize signal transduction. Our observations indicate that optimized p27kip1-mediated signaling originates from a combination of adaptive folding, and the cooperativity between its residual disorder and the functional collective motions of the CDK2–CA complex.

Graphical abstract: Dynamic optimization of signal transductionvia intrinsic disorder

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Publication details

The article was received on 02 Oct 2011, accepted on 27 Oct 2011 and first published on 14 Nov 2011


Article type: Communication
DOI: 10.1039/C1MB05412K
Mol. BioSyst., 2012,8, 194-197

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    Dynamic optimization of signal transductionvia intrinsic disorder

    L. M. Espinoza-Fonseca, Mol. BioSyst., 2012, 8, 194
    DOI: 10.1039/C1MB05412K

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