ArticleProtein science : a publication of the Protein Society1997
Oligomerization state of S100B at nanomolar concentration determined by large-zone analytical gel filtration chromatography.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 57 citations in OpenAlex.
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- Interferon-β Activity Is Affected by S100B Protein.International journal of molecular sciences · 2022Article
- Computational Design of Macrocyclic Binders of S100B(ββ): Novel Peptide Theranostics.Molecules (Basel, Switzerland) · 2021Article
- Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.The Journal of biological chemistry · 2012Article
- Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasion.Biochemistry · 2011Article
- Molecular determinants of S100B oligomer formation.PloS one · 2011Article
- Modulation of quaternary structure of S100 proteins by calcium ions.Biophysical chemistry · 2010Article
- The effects of CapZ peptide (TRTK-12) binding to S100B-Ca2+ as examined by NMR and X-ray crystallography.Journal of molecular biology · 2010Article
- The Calcium-Dependent Interaction of S100B with Its Protein Targets.Cardiovascular psychiatry and neurology · 2010Article
- Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers.The Journal of biological chemistry · 2009Article
- S100A1: Structure, Function, and Therapeutic Potential.Current chemical biology · 2009Article
- Novel interaction of the dopamine D2 receptor and the Ca2+ binding protein S100B: role in D2 receptor function.Molecular pharmacology · 2008Article
- Calcium-dependent and -independent interactions of the S100 protein family.The Biochemical journal · 2006Review
- Glial S100B Positive Vacuoles In Purkinje Cells: Earliest Morphological Abnormality In SCA1 Transgenic Mice.Journal of neurological sciences (Turkish) · 2006Article
- Structural changes in the C-terminus of Ca2+-bound rat S100B (beta beta) upon binding to a peptide derived from the C-terminal regulatory domain of p53.Protein science : a publication of the Protein Society · 1999Article
- High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins.Journal of biomolecular NMR · 1999Article
- S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.Protein science : a publication of the Protein Society · 1998Article
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4 authors at 2 institutions in 1 country.
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Abstract
S100B is a Ca(2+)-binding protein known to be a non-covalently associated dimer, S100B(beta beta), at high concentrations (0.2-3.0 mM) under reducing conditions. The solution structure of apo-S100B (beta beta) shows that the subunits associate in an antiparallel manner to form a tightly packed hydrophobic core at the dimer interface involving six of eight helices and the C-terminal loop (Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ. 1996. Solution structure of rat apo-S100B (beta beta) as determined by NMR spectroscopy. Biochemistry 35:11577-11588). The C-terminal loop, however, is also known to participate in the binding of S100B to target proteins, so its participation in the dimer interface raises questions as to the physiological relevance of dimeric S100B (beta beta). Therefore, we investigated the oligomerization state of S100B at low concentrations (1-10,000 nM) using large-zone analytical gel filtration chromatography with 35S-labeled S100B. We found that S100B exists (> 99%) as a non-covalently associated dimer, S100B (beta beta), at 1 nM subunit concentration (500 pM dimer) in the presence or absence of saturating levels of Ca2+, which implies a dissociation constant in the picomolar range or lower. These results demonstrate for the first time that in reducing environments and at physiological concentrations, S100B exists as dimeric S100B (beta beta) in the presence or absence of Ca2+, and that the non-covalent dimer is most likely the form of S100B presented to target proteins.
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