Considering the importance of the pH in modulating annexin activities, we here reassessed the pH dependency (range 4.6-7.4) of the binding of the calcium by human annexin A4 (hAnxA4) and determined its structure from crystals obtained in acidic conditions at nearly atomic resolution in media containing different calcium concentrations.

Computational, crystallographic, and biophysical characterizations provide insights into calcium and phosphate binding by human annexin A4

Vitagliano Luigi;Ruggiero Alessia
2025

Abstract

Considering the importance of the pH in modulating annexin activities, we here reassessed the pH dependency (range 4.6-7.4) of the binding of the calcium by human annexin A4 (hAnxA4) and determined its structure from crystals obtained in acidic conditions at nearly atomic resolution in media containing different calcium concentrations.
2025
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli Via Pietro Castellino 111
Annexin protein familyAnnexin A4Calcium/phospholipid-binding proteinsCrystal structureMolecular dockingMolecular dynamicsMetadynamics
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/554830
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