Sangam: A Confluence of Knowledge Streams

Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics

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dc.creator Pandini, A
dc.creator Fornili, A
dc.creator Fraternali, F
dc.creator Kleinjung, J
dc.date 2015-02-03T11:28:15Z
dc.date 2012-02
dc.date 2015-02-03T11:28:15Z
dc.date 2012
dc.date.accessioned 2022-05-25T14:53:41Z
dc.date.available 2022-05-25T14:53:41Z
dc.identifier FASEB Journal, 26:2, pp. 868 - 881, 2012
dc.identifier 0892-6638
dc.identifier http://www.fasebj.org/content/26/2/868
dc.identifier http://bura.brunel.ac.uk/handle/2438/10077
dc.identifier http://dx.doi.org/10.1096/fj.11-190868
dc.identifier.uri http://localhost:8080/xmlui/handle/CUHPOERS/172688
dc.description Allostery offers a highly specific way to modulate protein function. Therefore, understanding this mechanism is of increasing interest for protein science and drug discovery. However, allosteric signal transmission is difficult to detect experimentally and to model because it is often mediated by local structural changes propagating along multiple pathways. To address this, we developed a method to identify communication pathways by an information- theoretical analysis of molecular dynamics simulations. Signal propagation was described as information exchange through a network of correlated local motions, modeled as transitions between canonical states of protein fragments. The method was used to describe allostery in two-component regulatory systems. In particular, the transmission from the allosteric site to the signaling surface of the receiver domain NtrC was shown to be mediated by a layer of hub residues. The location of hubs preferentially connected to the allosteric site was found in close agreement with key residues experimentally identified as involved in the signal transmission. The comparison with the networks of the homologues CheY and FixJ highlighted similarities in their dynamics. In particular, we showed that a preorganized network of fragment connections between the allosteric and functional sites exists already in the inactive state of all three proteins. © The Author(s).
dc.format 868 - 881
dc.format 868 - 881
dc.language eng
dc.language en
dc.relation FASEB Journal
dc.relation FASEB Journal
dc.subject Molecular simulation
dc.subject Networks
dc.subject Structural alphabet
dc.subject Two-component systems
dc.title Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics
dc.type Article


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