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Article

The optimal docking strength for reversibly tethered kinases.

Proceedings of the National Academy of Sciences of the United States of America - 21 Jun 2022

Dyla Mateusz, González Foutel Nicolás S, Otzen Daniel E, Kjaergaard Magnus

Abstract excerpt

Many kinases use reversible docking interactions to augment the specificity of their catalytic domains. Such docking interactions are often structurally independent of the catalytic domain, which allow for a flexible combination of modules in evolution and in bioengineering. The affinity of docking interactions spans several orders of magnitude. This led us to ask how the affinity of the docking interaction...

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Share to Catalytic Domain
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 35696590
DOI: 10.1073/pnas.2203098119
PMCID: PMC9231604

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