{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Juarez-Romero GU"],"pubmed_abstract":["Tau protein is a microtubule-associated protein central to the pathogenesis of Alzheimer's disease (AD) and other tauopathies. While metal ion homeostasis is disrupted in AD, the presence of copper and zinc in neurofibrillary tangles suggests a pathological role for metal-tau interactions. In this study, the metal binding properties of Tau441 were probed using a wide range of spectroscopic tools. Specifically, electron paramagnetic resonance, circular dichroism, nuclear magnetic resonance (NMR) and X-ray absorption spectroscopy (XAS) results point to a single high-affinity Cu<sup>2+</sup> binding site within the microtubule-binding domain (MTBD), coordinated by the bis-His motif in R3 (His329/His330), possibly His299 and an oxygen-based ligand. This complex can be reduced resulting in a tr"],"journal":["Chemical science"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12917501"],"repository":["biostudies-literature"],"pubmed_title":["Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation."],"pmcid":["PMC12917501"],"pubmed_authors":["Quintanar L","Luo J","Gerez JA","Juarez-Romero GU","Nachtegaal M","Riek R","Sun X","Landrot G","Den Auwer C"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation.","description":"Tau protein is a microtubule-associated protein central to the pathogenesis of Alzheimer's disease (AD) and other tauopathies. While metal ion homeostasis is disrupted in AD, the presence of copper and zinc in neurofibrillary tangles suggests a pathological role for metal-tau interactions. In this study, the metal binding properties of Tau441 were probed using a wide range of spectroscopic tools. Specifically, electron paramagnetic resonance, circular dichroism, nuclear magnetic resonance (NMR) and X-ray absorption spectroscopy (XAS) results point to a single high-affinity Cu<sup>2+</sup> binding site within the microtubule-binding domain (MTBD), coordinated by the bis-His motif in R3 (His329/His330), possibly His299 and an oxygen-based ligand. This complex can be reduced resulting in a tr","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T17:58:41.57Z","creation":"2026-07-09T11:10:49.077Z"},"accession":"S-EPMC12917501","cross_references":{"pubmed":["41727718"],"doi":["10.1039/d5sc08604c"]}}