ArticleActa crystallographica. Section D, Biological crystallography2015
Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B-RAGE-derived peptide complex.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- TAT-W61 peptide attenuates neuronal injury through blocking the binding of S100b to the V-domain of Rage during ischemic stroke.Journal of molecular medicine (Berlin, Germany) · 2024Article
- Computational Design of Macrocyclic Binders of S100B(ββ): Novel Peptide Theranostics.Molecules (Basel, Switzerland) · 2021Article
- The Trp triad within the V-domain of the receptor for advanced glycation end products modulates folding, stability and ligand binding.Bioscience reports · 2020Article
- The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.Science advances · 2018Article
- Structural Basis for S100B Interaction with its Target Proteins.Journal of molecular and genetic medicine : an international journal of biomedical research · 2018Article
- X-ray crystal structure of human calcium-bound S100A1.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Blocking the Interactions between Calcium-Bound S100A12 Protein and the V Domain of RAGE Using Tranilast.PloS one · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
S100B is a damage-associated molecular pattern protein that, when released into the extracellular milieu, triggers initiation of the inflammatory response through the receptor for advanced glycation end products (RAGE). Recognition of S100B is accomplished via the amino-terminal variable immunoglobulin domain (V-domain) of RAGE. To gain insights into this interaction, a complex between S100B and a 15-amino-acid peptide derived from residues 54-68 of the V-domain was crystallized. The X-ray crystal structure was solved to 2.55 Å resolution. There are two dimers of S100B and one peptide in the asymmetric unit. The binding interface of this peptide is compared with that found in the complex between S100B and the 12-amino-acid CapZ-derived peptide TRTK-12. This comparison reveals that although the peptides adopt completely different backbone structures, the residues buried at the interface interact with S100B in similar regions to form stable complexes. The binding affinities of S100B for the intact wild-type V-domain and a W61A V-domain mutant were determined to be 2.7 ± 0.5 and 1.3 ± 0.7 µM, respectively, using fluorescence titration experiments. These observations lead to a model whereby conformational flexibility in the RAGE receptor allows the adoption of a binding conformation for interaction with the stable hydrophobic groove on the surface of S100B.
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