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Galectin-3 binds to the RGD-binding site in a glycan-independent manner and to the allosteric site and activates integrins αvβ3, αIIbβ3, and α5β1

2026-02-07

Abstract excerpt

Galectin-3 (Gal3) is one of the most pro-inflammatory proteins and a biomarker of inflammatory diseases and cancer. Previous studies showed that Gal3 binds to αv and β1 integrins but it is unclear how Gal3 binds to integrins. Here, we show that Gal3 bound to soluble αvβ3 and αIIbβ3 integrins in 1 mM Mn 2+ in cell-free conditions in a glycan-independent manner. Docking simulation predicts that Gal3 binds to the cl...

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Literature Corpus work
b1a0fed4-cd59-50ad-9cae-d7ba4af6e13b
DOI
10.64898/2026.02.05.704096
Open publication

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Galectin-3 binds to the RGD-binding site in a glycan-independent manner and to the allosteric site and activates integrins αvβ3, αIIbβ3, and α5β1DOI 10.64898/2026.02.05.704096
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