ArticleBMC structural biology2016
Crystal structure of human S100A8 in complex with zinc and calcium.
Article in BMC structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- The Role of S100A8/A9 in Autoimmune Eye Diseases: From Pathogenesis to Targeted Therapy.Investigative ophthalmology & visual science · 2026Review
- S100A9 deletion ameliorates acute lung injury by attenuating excessive neutrophil activation via activating the NRF2/HO-1 signaling axis.Respiratory research · 2026Article
- A proteomics approach to understand the hypomineralisation of second primary molars (HSPM). In-vitro study.European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry · 2025Article
- Relationship of S100 Proteins with Neuroinflammation.Biomolecules · 2025Review
- Exonic splicing code and coordination of divalent metals in proteins.Nucleic acids research · 2024Article
- Asthma-protective agents in dust from traditional farm environments.The Journal of allergy and clinical immunology · 2023Article
- S100 Proteins as Novel Therapeutic Targets in Psoriasis and Other Autoimmune Diseases.Molecules (Basel, Switzerland) · 2022Review
- Regulation of zinc-dependent enzymes by metal carrier proteins.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Review
- Label-free quantitative proteomics reveals molecular correlates of altered biomechanical properties in molar incisor hypomineralization (MIH): an in vitro study.European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry · 2022Article
- Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin.Journal of the American Chemical Society · 2021Article
- Identification of differentially expressed proteins involved in fetal scarless wound healing using a rat model of cleft lip.Molecular medicine reports · 2021Article
- Article
- Molecular Dynamics Investigation into the Effect of Zinc(II) on the Structure and Membrane Interactions of the Antimicrobial Peptide Clavanin A.The journal of physical chemistry. B · 2019Article
- Article
- Regulation of Three Virulence Strategies of Mycobacterium tuberculosis: A Success Story.International journal of molecular sciences · 2018Review
- Solving the crystal structure of human calcium-free S100Z: the siege and conquer of one of the last S100 family strongholds.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundS100 proteins are a large family of calcium binding proteins present only in vertebrates. They function intra- and extracellularly both as regulators of homeostatic processes and as potent effectors during inflammation. Among these, S100A8 and S100A9 are two major constituents of neutrophils that can assemble into homodimers, heterodimers and higher oligomeric species, including fibrillary structures found in the ageing prostate. Each of these forms assumes specific functions and their formation is dependent on divalent cations, notably calcium and zinc. In particular, zinc appears as a major regulator of S100 protein function in a disease context. Despite this central role, no structural information on how zinc bind to S100A8/S100A9 and regulates their quaternary structure is yet available.
resultsHere we report two crystallographic structures of calcium and zinc-loaded human S100A8. S100A8 binds two zinc ions per homodimer, through two symmetrical, all-His tetracoordination sites, revealing a classical His-Zn binding mode for the protein. Furthermore, the presence of a (Zn)2-cacodylate complex in our second crystal form induces ligand swapping within the canonical His4 zinc binding motif, thereby creating two new Zn-sites, one of which involves residues from symmetry-related molecules. Finally, we describe the calcium-induced S100A8 tetramer and reveal how zinc stabilizes this tetramer by tightening the dimer-dimer interface.
conclusionsOur structures of Zn(2+)/Ca(2+)-bound hS100A8 demonstrate that S100A8 is a genuine His-Zn S100 protein. Furthermore, they show how zinc stabilizes S100A8 tetramerization and potentially mediates the formation of novel interdimer interactions. We propose that these zinc-mediated interactions may serve as a basis for the generation of larger oligomers in vivo.
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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.