ArticlePloS one2014
Structural insights into calcium-bound S100P and the V domain of the RAGE complex.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Network of interactions between the tumor necrosis factor superfamily members and small S100 proteins.PloS one · 2026Article
- Modulation of Aging Diseases via RAGE Targets: A Dietary Intervention Review.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Relationship of S100 Proteins with Neuroinflammation.Biomolecules · 2025Review
- cPEPmatch Webserver: A comprehensive tool and database to aid rational design of cyclic peptides for drug discovery.Computational and structural biotechnology journal · 2024Article
- Molecular Basis for the Involvement of Mammalian Serum Albumin in the AGE/RAGE Axis: A Comprehensive Computational Study.International journal of molecular sciences · 2024Article
- An Extracellular/Membrane-Bound S100P Pool Regulates Motility and Invasion of Human Extravillous Trophoblast Lines and Primary Cells.Biomolecules · 2023Article
- Calcium-Bound S100P Protein Is a Promiscuous Binding Partner of the Four-Helical Cytokines.International journal of molecular sciences · 2022Article
- Therapeutic potential of targeting the receptor for advanced glycation end products (RAGE) by small molecule inhibitors.Drug development research · 2022Review
- Calcium-binding protein S100P is a new target gene of MACC1, drives colorectal cancer metastasis and serves as a prognostic biomarker.British journal of cancer · 2022Article
- Pathophysiology of RAGE in inflammatory diseases.Frontiers in immunology · 2022Review
- The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis.Biomolecules · 2021Article
- Hypoxia and the Receptor for Advanced Glycation End Products (RAGE) Signaling in Cancer.International journal of molecular sciences · 2021Review
- Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes.Frontiers in molecular biosciences · 2021Review
- Discovery of novel small molecule inhibitors of S100P with in vitro anti-metastatic effects on pancreatic cancer cells.European journal of medicinal chemistry · 2020Article
- CD146, from a melanoma cell adhesion molecule to a signaling receptor.Signal transduction and targeted therapy · 2020Review
- Direct interaction of metastasis-inducing S100P protein with tubulin causes enhanced cell migration without changes in cell adhesion.The Biochemical journal · 2020Article
- The Trp triad within the V-domain of the receptor for advanced glycation end products modulates folding, stability and ligand binding.Bioscience reports · 2020Article
- Calcium-Binding Protein S100P Promotes Tumor Progression but Enhances Chemosensitivity in Breast Cancer.Frontiers in oncology · 2020Article
- Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain.PloS one · 2019Article
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Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The S100P protein is a member of the S100 family of calcium-binding proteins and possesses both intracellular and extracellular functions. Extracellular S100P binds to the cell surface receptor for advanced glycation end products (RAGE) and activates its downstream signaling cascade to meditate tumor growth, drug resistance and metastasis. Preventing the formation of this S100P-RAGE complex is an effective strategy to treat various disease conditions. Despite its importance, the detailed structural characterization of the S100P-RAGE complex has not yet been reported. In this study, we report that S100P preferentially binds to the V domain of RAGE. Furthermore, we characterized the interactions between the RAGE V domain and Ca(2+)-bound S100P using various biophysical techniques, including isothermal titration calorimetry (ITC), fluorescence spectroscopy, multidimensional NMR spectroscopy, functional assays and site-directed mutagenesis. The entropy-driven binding between the V domain of RAGE and Ca(+2)-bound S100P was found to lie in the micromolar range (Kd of ∼ 6 µM). NMR data-driven HADDOCK modeling revealed the putative sites that interact to yield a proposed heterotetrameric model of the S100P-RAGE V domain complex. Our study on the spatial structural information of the proposed protein-protein complex has pharmaceutical relevance and will significantly contribute toward drug development for the prevention of RAGE-related multifarious diseases.
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