Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?
Sign Up to like & getrecommendations! Published in 2018 at "Protein Science"
DOI: 10.1002/pro.3475
Abstract: There are many multidomain allosteric proteins where an allosteric signal at the allosteric domain modifies the activity of the functional domain. Intrinsically disordered regions (linkers) are widely involved in this kind of regulation process, but… read more here.
Keywords: state; allosteric proteins; favor; multidomain allosteric ... See more keywords
Protein topology and allostery.
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DOI: 10.1016/j.sbi.2020.01.011
Abstract: Allostery plays important roles in many biological processes. Although all non-fibrous proteins may be allosteric, currently only a limited number of allosteric proteins are known. How allosteric regulation depends on protein topology and what are… read more here.
Keywords: topology; allosteric proteins; topology allostery; protein topology ... See more keywords
Epistasis shapes the fitness landscape of an allosteric specificity switch
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DOI: 10.1038/s41467-021-25826-7
Abstract: Epistasis is a major determinant in the emergence of novel protein function. In allosteric proteins, direct interactions between inducer-binding mutations propagate through the allosteric network, manifesting as epistasis at the level of biological function. Elucidating… read more here.
Keywords: fitness landscape; allosteric proteins; epistasis shapes; specificity ... See more keywords