Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 71, Issue -, Pages 1176-1183Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1399004715004216
Keywords
S100B; RAGE-derived peptide
Funding
- National Institutes of Health [P20 RR015566, P30 GM103332-01]
- National Science Foundation [EPS-0814442]
- Infrastructure Improvement Program-Doctoral Dissertation Assistantship (IIP-DDA), North Dakota EPSCoR Grant: NSF [0814442]
- National Institute of General Medical Sciences from the National Institutes of Health [P41 GM103403]
- DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
- EPSCoR
- Office Of The Director [0814442] Funding Source: National Science Foundation
- Office Of The Director
- Office of Integrative Activities [1355466] Funding Source: National Science Foundation
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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 angstrom 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 mu M, 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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