ArticleBiochemistry2012
Reactive cysteine in the structural Zn(2+) site of the C1B domain from PKCα.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Folding and unfolding dynamics of a DNA aptamer studied by heteronuclearJournal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Determination of Structural Factors Contributing to Protection of Zinc Fingers in Estrogen Receptor α through Molecular Dynamic Simulations.The journal of physical chemistry. B · 2025Article
- The Pseudomonas aeruginosa PAO1 metallo flavoprotein d-2-hydroxyglutarate dehydrogenase requires ZnThe Journal of biological chemistry · 2023Article
- Uncovering ZnThe Journal of biological chemistry · 2023Article
- Redox proteomic study of Bacillus cereus thiol proteome during fermentative anaerobic growth.BMC genomics · 2021Article
- Protein Lipoxidation: Basic Concepts and Emerging Roles.Antioxidants (Basel, Switzerland) · 2021Review
- Reactivity of Thiol-Rich Zn Sites in Diacylglycerol-Sensing PKC C1 Domain Probed by NMR Spectroscopy.Frontiers in molecular biosciences · 2021Article
- Toggling of Diacylglycerol Affinity Correlates with Conformational Plasticity in C1 Domains.Biochemistry · 2017Article
- Classification of the treble clef zinc finger: noteworthy lessons for structure and function evolution.Scientific reports · 2016Article
- Dynamics and Membrane Interactions of Protein Kinase C.Biochemistry · 2015Review
- Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks.Chemistry & biology · 2015Article
- A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage.Journal of the American Chemical Society · 2014Article
- Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions.Redox biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Structural cysteine-rich Zn(2+) sites that stabilize protein folds are considered to be unreactive. In this article, we identified a reactive cysteine residue, Cys151, in a treble-clef zinc finger with a Cys(3)His coordination sphere. The protein in question is the C1B domain of Protein Kinase Cα (PKCα). Mass-tagging cysteine assays of several C1B variants were employed to ascertain the site specificity of the covalent modification. The reactivity of Cys151 in C1B also manifests itself in the structural dynamics of the Zn(2+) coordination sphere where the Sγ of Cys151 alternates between the Zn(2+)-bound thiolate and free thiol states. We used NMR-detected pH titrations, ZZ-exchange spectroscopy, and residual dipolar coupling (RDC)-driven structure refinement to characterize the two exchanging conformations of C1B that differ in zinc coordination. Our data suggest that Cys151 serves as an entry point for the reactive oxygen species that activate PKCα in a process involving Zn(2+) release.
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Registered trials
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.