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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I03-Macromolecular Crystallography I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Lessons from LIMK1 enzymology and their impact on inhibitor design Eidarus Salah , Deep Chatterjee , Alessandra Beltrami , Anthony Tumber , Franziska Preuss , Peter Canning , Apirat Chaikuad , Petra Knaus , Stefan Knapp , Alex N. Bullock , Sebastian Mathea Biochemical Journal DOI: 10.1042/BCJ20190517 Diamond Proposal Number(s): [6391, 10619] Show Abstract ▼ Abstract: LIM domain kinase 1 (LIMK1) is a key regulator of actin dynamics. It is thereby a potential therapeutic target for the prevention of fragile X syndrome and amyotrophic lateral sclerosis. Herein, we use X-ray crystallography and activity assays to describe how LIMK1 accomplishes substrate specificity, to suggest a unique 'rock-and-poke' mechanism of catalysis and to explore the regulation of the kinase by activation loop phosphorylation. Based on these findings, a differential scanning fluorimetry assay and a RapidFire mass spectrometry activity assay were established, leading to the discovery and confirmation of a set of small-molecule LIMK1 inhibitors. Interestingly, several of the inhibitors were inactive towards the closely related isoform LIMK2. Finally, crystal structures of the LIMK1 kinase domain in complex with inhibitors (PF-477736 and staurosporine, respectively) are presented, providing insights into LIMK1 plasticity upon inhibitor binding.	Oct 2019

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