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- W4313455141 abstract "Allosteric pathways in proteins describe networks comprising amino acid residues which may facilitate the propagation of signals between distant sites. Through inter-residue interactions, dynamic and conformational changes can be transmitted from the site of perturbation to an allosteric site. While sophisticated computational methods have been developed to characterize such allosteric pathways linking specific sites on proteins, few attempts have been made to apply these approaches toward identifying new allosteric sites. Here, we use molecular dynamics simulations and suboptimal path analysis to discover new allosteric networks in steroid receptors with a focus on evolutionarily conserved pathways. Using modern receptors and a reconstructed ancestral receptor, we identify networks connecting several sites to the activation function surface 2 (AF-2), the site of coregulator recruitment. One of these networks is conserved across the entire family, connecting a predicted allosteric site located between helices 9 and 10 of the ligand-binding domain. We investigate the basis of this conserved network as well as the importance of this site, discovering that the site lies in a region of the ligand-binding domain characterized by conserved inter-residue contacts. This study suggests an evolutionarily importance of the helix 9-helix 10 site in steroid receptors and identifies an approach that may be applied to discover previously unknown allosteric sites in proteins." @default.
- W4313455141 created "2023-01-06" @default.
- W4313455141 creator A5002677131 @default.
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- W4313455141 date "2023-01-03" @default.
- W4313455141 modified "2023-10-14" @default.
- W4313455141 title "Identification of an Evolutionarily Conserved Allosteric Network in Steroid Receptors" @default.
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- W4313455141 doi "https://doi.org/10.1021/acs.jcim.2c01096" @default.
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- W4313455141 hasPublicationYear "2023" @default.
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