2015
DOI: 10.1093/nar/gkv902
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Abstract: Allosteric regulation, the most direct and efficient way of regulating protein function, is induced by the binding of a ligand at one site that is topographically distinct from an orthosteric site. Allosteric Database (ASD, available online at http://mdl.shsmu.edu.cn/ASD) has been developed to provide comprehensive information featuring allosteric regulation. With increasing data, fundamental questions pertaining to allostery are currently receiving more attention from the mechanism of allosteric changes in an… Show more

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Cited by 114 publications
(118 citation statements)
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“…Allosteric modulators of ligand‐gated ion channels are assumed to affect the pathways that pair agonist binding to channel gating. A large number of allosteric modulators has been identified for neuronal‐type nACh receptors (see AlloSteric Database (ASD)). An allosteric mechanism of channel blockage by HC for muscle‐type receptor has been proposed by Bouzat and Barrantes .…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Allosteric modulators of ligand‐gated ion channels are assumed to affect the pathways that pair agonist binding to channel gating. A large number of allosteric modulators has been identified for neuronal‐type nACh receptors (see AlloSteric Database (ASD)). An allosteric mechanism of channel blockage by HC for muscle‐type receptor has been proposed by Bouzat and Barrantes .…”
Section: Discussionmentioning
confidence: 99%
“…Studies based on statistical methods, that were used to compare large databases of cancer genomes suggest that somatic mutations in allosteric and orthosteric sites are more likely to initiate tumor growth than in other sites in these proteins . Allosteric proteins are also attractive targets in drug design research . Modulating receptors via allosteric sites is suggested to be more effective in therapeutic application than via othosteric sites because of lesser adverse effect.…”
Section: Discussionmentioning
confidence: 99%
“…We also accessed all the proteins associated with allostery in the AlloSteric Database 59 . Allosteric proteins are listed in Table S2.…”
Section: Methodsmentioning
confidence: 99%
“…Docking results showed that the coptisine binding site is highly variable in amino acid sequence between the enzymes from the two species, most of all, two key amino acids which have been identified as the "species-selective inhibitor site" of HsDHODH Met43 and Ala59 are replaced by Leu172 and Phe188 in PfDHODH, respectively. [42] Moreover, the interactions between coptisine with PfDHODH or HsDHODH were largely based on the oxygen atom of 1,3-benzodioxole; meanwhile, several 1,3-benzodioxole relevant compounds have been reported with antioxidative, antitumor, and antimicrobial activities. Further, compared the putative binding mode of coptisine in PfDHODH with the crystal structure of A77 1726 within PfDHODH (PDB 1TV5), we noticed a conformational change in the position of Phe188 between the two structures caused different binding modes.…”
Section: Discussionmentioning
confidence: 99%