Substrate promiscuity of inositol 1,4,5-trisphosphate kinase driven by structurally-modified ligands and active site plasticity

Substrate promiscuity of inositol 1,4,5-trisphosphate kinase driven by structurally-modified ligands and active site plasticity

Abstract d-myo-inositol 1,4,5-trisphosphate (InsP3) is a fundamental second messenger in cellular Ca2+ mobilization. InsP3 3-kinase, a highly specific enzyme binding InsP3 in just one mode, phosphorylates InsP3 specifically at its secondary 3-hydroxyl group to generate a tetrakisphosphate. Using a c...

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Bibliographic Details
Main Authors: María Ángeles Márquez-Moñino, Raquel Ortega-García, Hayley Whitfield, Andrew M. Riley, Lourdes Infantes, Shane W. Garrett, Megan L. Shipton, Charles A. Brearley, Barry V. L. Potter, Beatriz González
Format: Article
Language:English
Published: Nature Portfolio 2024-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-024-45917-5

Internet

https://doi.org/10.1038/s41467-024-45917-5

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