Supplementary data to "Ligand binding site structure shapes allosteric signal transduction and the evolution of allostery in protein complexes" by G. Abrusan and J.A. Marsh
Depositor | dc.contributor | Abrusan, Gyorgy | |
Funder | dc.contributor.other | MRC - Medical Research Council | en_UK |
Data Creator | dc.creator | Abrusan, Gyorgy | |
Data Creator | dc.creator | Marsh, Joseph | |
Date Accessioned | dc.date.accessioned | 2019-02-04T17:13:13Z | |
Date Available | dc.date.available | 2019-02-04T17:13:13Z | |
Citation | dc.identifier.citation | Abrusan, Gyorgy; Marsh, Joseph. (2019). Supplementary data to "Ligand binding site structure shapes allosteric signal transduction and the evolution of allostery in protein complexes" by G. Abrusan and J.A. Marsh, [dataset]. University of Edinburgh. MRC Human Genetics Unit. https://doi.org/10.7488/ds/2493. | en |
Persistent Identifier | dc.identifier.uri | http://hdl.handle.net/10283/3253 | |
Persistent Identifier | dc.identifier.uri | https://doi.org/10.7488/ds/2493 | |
Dataset Description (abstract) | dc.description.abstract | The structure of ligand binding sites has been shown to profoundly influence the evolution of function in homomeric protein complexes. Complexes with multi-chain binding sites (MBSs) have more conserved quaternary structure, more similar binding sites and ligands between homologues, and evolve new functions slower than homomers with single-chain binding sites (SBSs). Here, using in silico analyses of protein dynamics, we investigate whether ligand binding-site structure shapes allosteric signal transduction pathways (STPs), and whether the structural similarity of binding sites influences the evolution of allostery. Our analyses show that: 1) allostery is more frequent among MBS complexes than in SBS complexes, particularly in homomers; 2) in MBS homomers, semi-rigid communities and critical residues frequently connect interfaces and thus they are characterized by STPs that cross protein-protein interfaces, while SBS homomers usually not; 3) ligand binding alters community structure differently in MBS and SBS homomers; 4) allosteric proteins are more likely to have homologs with similar binding site than non-allosteric proteins, suggesting that binding site similarity is an important factor driving the evolution of allostery. | en_UK |
Language | dc.language.iso | eng | en_UK |
Publisher | dc.publisher | University of Edinburgh. MRC Human Genetics Unit | en_UK |
Rights | dc.rights | Creative Commons Attribution 4.0 International Public License | en |
Subject | dc.subject | quaternary structure | en_UK |
Subject | dc.subject | evolution of allostery | en_UK |
Subject | dc.subject | critical residues | en_UK |
Subject | dc.subject | communities | en_UK |
Subject | dc.subject | ligand binding | en_UK |
Subject Classification | dc.subject.classification | Biological Sciences::Biomolecular Science | en_UK |
Title | dc.title | Supplementary data to "Ligand binding site structure shapes allosteric signal transduction and the evolution of allostery in protein complexes" by G. Abrusan and J.A. Marsh | en_UK |
Type | dc.type | dataset | en_UK |
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