ArticleProtein science : a publication of the Protein Society2002
Conformational and thermodynamic properties of peptide binding to the human S100P protein.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- Melittin, A Potential Game-changer in the Fight Against Breast Cancer: A Systematic Review.Anti-cancer agents in medicinal chemistry · 2025Pooled it
- Review
- Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin.Protein science : a publication of the Protein Society · 2014Article
- Article
- 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
- Identification of calcium-independent and calcium-enhanced binding between S100B and the dopamine D2 receptor.Biochemistry · 2011Article
- Modulation of quaternary structure of S100 proteins by calcium ions.Biophysical chemistry · 2010Article
- Annexin I and annexin II N-terminal peptides binding to S100 protein family members: specificity and thermodynamic characterization.Biochemistry · 2009Article
- Hydrophobic interactions are the driving force for the binding of peptide mimotopes and Staphylococcal protein A to recombinant human IgG1.European biophysics journal : EBJ · 2007Article
- Calcium-dependent and -independent interactions of the S100 protein family.The Biochemical journal · 2006Review
- Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin alphaIIb cytoplasmic domain.Protein science : a publication of the Protein Society · 2005Article
- Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer.The American journal of pathology · 2005Article
- NMR structure of the Apo-S100P protein.Journal of biomolecular NMR · 2004Article
- Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P.Molecular biology of the cell · 2003Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
S100P is a member of the S100 subfamily of calcium-binding proteins that are believed to be associated with various diseases, and in particular deregulation of S100P expression has been documented for prostate and breast cancer. Previously, we characterized the effects of metal binding on the conformational properties of S100P and proposed that S100P could function as a Ca2+ conformational switch. In this study we used fluorescence and CD spectroscopies and isothermal titration calorimetry to characterize the target-recognition properties of S100P using a model peptide, melittin. Based on these experimental data we show that S100P and melittin can interact in a Ca2+-dependent and -independent manner. Ca2+-independent binding occurs with low affinity (Kd approximately 0.2 mM), has a stoichiometry of four melittin molecules per S100P dimer and is presumably driven by favorable electrostatic interactions between the acidic protein and the basic peptide. In contrast, Ca2+-dependent binding of melittin to S100P occurs with high affinity (Kd approximately 5 microM) has a stoichiometry of two molecules of melittin per S100P dimer, appears to have positive cooperativity, and is driven by hydrophobic interactions. Furthermore, Ca2+-dependent S100P-melittin complex formation is accompanied by significant conformational changes: Melittin, otherwise unstructured in solution, adopts a helical conformation upon interaction with Ca2+-S100P. These results support a model for the Ca2+-dependent conformational switch in S100P for functional target recognition.
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