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- W2761066511 abstract "Hidden allosteric sites, as a novel type of allosteric site, are invisible in ligand-unbound (apo) crystal structures, but can emerge in ligand-bound (holo) crystal structures when a specific ligand binds to, and stabilizes, a unique conformation favored by the ligand. However, the identification of these sites is a significant challenge. Several computational and experimental approaches have been developed to identify such sites in proteins. Here, we outline these approaches, with a focus on examples of the successful use of such techniques. The discovery of hidden allosteric sites offers a new avenue for facilitating drug design by greatly expanding the repertoire of available drug targets, contributing to the search for allosteric drugs for the treatment of human diseases." @default.
- W2761066511 created "2017-10-20" @default.
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- W2761066511 date "2018-02-01" @default.
- W2761066511 modified "2023-09-25" @default.
- W2761066511 title "Discovery of hidden allosteric sites as novel targets for allosteric drug design" @default.
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- W2761066511 doi "https://doi.org/10.1016/j.drudis.2017.10.001" @default.
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