ArticleJournal of structural biology: X2026
FHL2 production enabled new insight into its flexibility and unexpected binding stoichiometry with β-catenin.
Article in Journal of structural biology: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Four-and-a-half LIM domains protein 2 (FHL2) is a modular adaptor composed entirely of LIM domains that mediate protein-protein interactions linking the cytoskeleton to transcriptional regulation. Here, we report a streamlined preparation of recombinant tag-free full-length FHL2 in bacteria and describe its biophysical characterization using size-exclusion chromatography coupled to static light scattering (SEC-SLS), small-angle X-ray scattering (SEC-SAXS), and cross-linking coupled with mass spectrometry (XL-MS). Soluble expression was enhanced by zinc supplementation and low-temperature induction. Purified FHL2 eluted from SEC-SLS as a monomeric species consistent with a flexible, elongated multidomain architecture. Integrative modeling based on SAXS and XL-MS confirmed that FHL2 exists in an extended and a compact bent conformation in solution. SEC-SLS and Isothermal titration calorimetry (ITC) measurements confirmed a direct 2:1 interaction between FHL2 and β-catenin with submicromolar affinity, supporting FHL2's scaffolding role within the Wnt/β-catenin signaling pathway. These results establish the groundwork for structural and functional analyses of FHL2 and related LIM-domain proteins.
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