A Cu(II) binding site involving Cys18 and His22 displays a buffering effect in copper-induced aggregation of cataract-related human γD crystallin.

doi:10.1016/j.jinorgbio.2026.113289

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Article

A Cu(II) binding site involving Cys18 and His22 displays a buffering effect in copper-induced aggregation of cataract-related human γD crystallin.

Journal of inorganic biochemistry - 1 Jul 2026

Uc-Santos Eusebio, Quintanar Liliana

Abstract excerpt

Cataracts are the main cause of blindness in the world, and they are caused by aggregation of lens crystallin proteins. Metal ions have emerged as a potential factor in the development of cataract disease, as copper and zinc ions induce the non-amyloid aggregation of lens crystallins in vitro. Copper-induced aggregation of human γD crystallin (HγD) involves disulfide and metal bridging, partial unfolding of the...

Topics

Humans
Copper
gamma-Crystallins
Binding Sites
Cataract
Cysteine
Histidine
Mutation
Protein Aggregates
Electron Spin Resonance Spectroscopy

Source

Open in PubMed

Identifiers

PMID: 41825345
DOI: 10.1016/j.jinorgbio.2026.113289

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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