ArticleThe Journal of biological chemistry2012
Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 71 citations in OpenAlex.
- Small heat shock protein HSPB5 uses disorder to bind zinc with high affinity.bioRxiv : the preprint server for biology · 2025Article
- The interaction of Cu(II) and Zn(II) with peptide fragment of HSPB1 and its analogs.Frontiers in molecular biosciences · 2025Article
- Celastrol regulates the oligomeric state and chaperone activity of αB-crystallin linked with protein homeostasis in the lens.Fundamental research · 2024Article
- Heat shock proteins and metal ions - Reaction or interaction?Computational and structural biotechnology journal · 2023Review
- Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus.Metallomics : integrated biometal science · 2022Article
- Review
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Peeking from behind the veil of enigma: emerging insights on small heat shock protein structure and function.Cell stress & chaperones · 2020Review
- Conditional Disorder in Small Heat-shock Proteins.Journal of molecular biology · 2020Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Mechanisms of Small Heat Shock Proteins.Cold Spring Harbor perspectives in biology · 2019Review
- Structural and functional consequences of age-related isomerization in α-crystallins.The Journal of biological chemistry · 2019Article
- Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.Cell stress & chaperones · 2017Article
- Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2015Article
- Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015Article
- The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Nature structural & molecular biology · 2015Article
- Facing and Overcoming Sensitivity Challenges in Biomolecular NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015Review
- Article
- Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.FEBS open bio · 2015Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human small heat-shock protein αB-crystallin (αB) rescues misfolded proteins from irreversible aggregation during cellular stress. Binding of Cu(II) was shown to modulate the oligomeric architecture and the chaperone activity of αB. However, the mechanistic basis of this stimulation is so far not understood. We provide here first structural insights into this Cu(II)-mediated modulation of chaperone function using NMR spectroscopy and other biophysical approaches. We show that the α-crystallin domain is the elementary Cu(II)-binding unit specifically coordinating one Cu(II) ion with picomolar binding affinity. Putative Cu(II) ligands are His(83), His(104), His(111), and Asp(109) at the dimer interface. These loop residues are conserved among different metazoans, but also for human αA-crystallin, HSP20, and HSP27. The involvement of Asp(109) has direct implications for dimer stability, because this residue forms a salt bridge with the disease-related Arg(120) of the neighboring monomer. Furthermore, we observe structural reorganization of strands β2-β3 triggered by Cu(II) binding. This N-terminal region is known to mediate both the intermolecular arrangement in αB oligomers and the binding of client proteins. In the presence of Cu(II), the size and the heterogeneity of αB multimers are increased. At the same time, Cu(II) increases the chaperone activity of αB toward the lens-specific protein β(L)-crystallin. We therefore suggest that Cu(II) binding unblocks potential client binding sites and alters quaternary dynamics of both the dimeric building block as well as the higher order assemblies of αB.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.