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Flexibility and electrostatic interactions on the coupled binding-folding mechanisms of Chz.core and H2A.z-H2B complex

Abstract

The intrinsically disordered protein (IDP) Chz.core, which is the interaction core of Chz1, shows the binding preference to histone variant H2A.z. Although there are several studies on this protein binding, the detailed coupled binding-folding processes are still not very clear. In this study, we explored the coupled binding-folding mechanism and the effect of flexibility by continuously monitoring the flexible degree of Chz.core. We applied the all-atom structure-based model (SBM), which can provide both backbone and sidechain information of the conformational change of Chz.core during binding. We provided a somewhat different "fly-casting" picture that long IDP can undergo a tertiary stretching and bending with larger capture radii than ordered protein. Our results suggest that the high flexibility of Chz.core contributes to the shorter times for capturing events, leading to higher recognition efficiency. In addition, compared to the ordered proteins, the high flexibility of intrinsically disordered protein enables the Chz.core to have lower binding barrier and faster association rate, which is favorable for the binding process to its partner H2A.z-H2B.

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Publication details

The article was received on 22 Feb 2017, accepted on 13 Jul 2017 and first published on 25 Jul 2017


Article type: Paper
DOI: 10.1039/C7MB00103G
Citation: Mol. BioSyst., 2017, Accepted Manuscript
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    Flexibility and electrostatic interactions on the coupled binding-folding mechanisms of Chz.core and H2A.z-H2B complex

    X. Shang, W. Chu, X. Chu, C. Liu, L. Xu and J. Wang, Mol. BioSyst., 2017, Accepted Manuscript , DOI: 10.1039/C7MB00103G

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