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Shelling the Voronoi interface of protein-protein complexes predicts residue activity and conservation

Abstract : The accurate description of protein-protein interfaces remains a challenging task. Traditional criteria, based on atomic contacts or changes in solvent accessibility, tend to over or underpredict the interface itself and cannot discriminate active from less relevant parts. A recent molecular dynamics simulation study by Mihalek and co-authors (2007, JMB 369, 584-95) concluded that active residues tend to be `dry', that is, insulated from water fluctuations. We show that patterns of `dry' residues can, to a large extent, be predicted by a fast, parameter-free and purely geometric analysis of protein interfaces. We introduce the shelling order of Voronoi facets as a straightforward quantitative measure of an atom's depth inside an interface. We analyze the correlation between Voronoi shelling order, dryness, and conservation on a set of 54 protein-protein complexes. Residues with high shelling order tend to be dry; evolutionary conservation also correlates with dryness and shelling order but, perhaps not surprisingly, is a much less accurate predictor of either property. Voronoi shelling order thus seems a meaningful and efficient descriptor of protein interfaces. Moreover, the strong correlation with dryness suggests that water dynamics within protein interfaces may, in first approximation, be described by simple diffusion models.
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Contributor : Frederic Cazals <>
Submitted on : Friday, January 18, 2008 - 9:03:36 AM
Last modification on : Monday, January 13, 2020 - 5:08:05 PM
Long-term archiving on: : Friday, November 25, 2016 - 8:07:35 PM


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  • HAL Id : inria-00206173, version 3



Benjamin Bouvier, Raik Gruenberg, Michael Nilges, Frédéric Cazals. Shelling the Voronoi interface of protein-protein complexes predicts residue activity and conservation. [Research Report] RR-6415, INRIA. 2008. ⟨inria-00206173v3⟩



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