ArticleProtein science : a publication of the Protein Society1999
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.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 40 citations in OpenAlex.
- Hierarchical AF2RAVE for Multiconformation Virtual Screening Targeting S100 CaJournal of chemical theory and computation · 2025Article
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- Specificity of Molecular Fragments Binding to S100B versus S100A1 as Identified by NMR and Site Identification by Ligand Competitive Saturation (SILCS).Molecules (Basel, Switzerland) · 2021Article
- The calcium-binding protein S100B reduces IL6 production in malignant melanoma via inhibition of RSK cellular signaling.PloS one · 2021Article
- Covalent small molecule inhibitors of Ca(2+)-bound S100B.Biochemistry · 2014Article
- Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide.Biopolymers · 2014Article
- Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization.Biochemistry · 2013Article
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Molecular dynamic simulation insights into the normal state and restoration of p53 function.International journal of molecular sciences · 2012Review
- In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction.International journal of high throughput screening · 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
- Small molecules bound to unique sites in the target protein binding cleft of calcium-bound S100B as characterized by nuclear magnetic resonance and X-ray crystallography.Biochemistry · 2009Article
- S100A1: Structure, Function, and Therapeutic Potential.Current chemical biology · 2009Article
- Solution structure of S100A1 bound to the CapZ peptide (TRTK12).Journal of molecular biology · 2009Article
- Structure of Ca2+-bound S100A4 and its interaction with peptides derived from nonmuscle myosin-IIA.Biochemistry · 2008Article
- S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling.The Journal of biological chemistry · 2008Article
- Calcium-dependent and -independent interactions of the S100 protein family.The Biochemical journal · 2006Review
- A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.The EMBO journal · 2001Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
S100B(beta beta) is a dimeric Ca2+-binding protein that interacts with p53, inhibits its phosphorylation by protein kinase C (PKC) and promotes disassembly of the p53 tetramer. Likewise, a 22 residue peptide derived from the C-terminal regulatory domain of p53 has been shown to interact with S100B(beta beta) in a Ca2+-dependent manner and inhibits its phosphorylation by PKC. Hence, structural studies of Ca2+-loaded S100B(beta beta) bound to the p53 peptide were initiated to characterize this interaction. Analysis of nuclear Overhauser effect (NOE) correlations, amide proton exchange rates, 3J(NH-H alpha) coupling constants, and chemical shift index data show that, like apo- and Ca2+-bound S100B(beta beta), S100B remains a dimer in the p53 peptide complex, and each subunit has four helices (helix 1, Glu2-Arg20; helix 2, Lys29-Asn38; helix 3, Gln50-Asp61; helix 4, Phe70-Phe87), four loops (loop 1, Glu21-His25; loop 2, Glu39-Glu49; loop 3, Glu62-Gly66; loop 4, Phe88-Glu91), and two beta-strands (beta-strand 1, Lys26-Lys28; beta-strand 2, Glu67-Asp69), which forms a short antiparallel beta-sheet. However, in the presence of the p53 peptide helix 4 is longer by five residues than in apo- or Ca2+-bound S100B(beta beta). Furthermore, the amide proton exchange rates in helix 3 (K55, V56, E58, T59, L60, D61) are significantly slower than those of Ca2+-bound S100B(beta beta). Together, these observations plus intermolecular NOE correlations between the p53 peptide and S100B(beta beta) support the notion that the p53 peptide binds in a region of S100B(beta beta), which includes residues in helix 2, helix 3, loop 2, and the C-terminal loop, and that binding of the p53 peptide interacts with and induces the extension of helix 4.
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