RGD Reference Report - Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis. - Rat Genome Database

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Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis.

Authors: Wilder, Paul T  Baldisseri, Donna M  Udan, Ryan  Vallely, Kristen M  Weber, David J 
Citation: Wilder PT, etal., Biochemistry. 2003 Nov 25;42(46):13410-21. doi: 10.1021/bi035334q.
RGD ID: 155888563
Pubmed: PMID:14621986   (View Abstract at PubMed)
DOI: DOI:10.1021/bi035334q   (Journal Full-text)

In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high affinity as confirmed using isothermal titration calorimetry (ITC; K(d) = 94 +/- 17 nM). The Zn(2+)-binding site on Ca(2+)-bound S100B was examined further using NMR spectroscopy and site-directed mutagenesis. Specifically, ITC measurements of S100B mutants (helix 1, H15A and H25A; helix 4, C84A, H85A, and H90A) were found to bind Zn(2+) with lower affinity than wild-type S100B (from 2- to >25-fold). Thus, His-15, His-25, Cys-84, His-85, and perhaps His-90 of S100B are involved in coordinating Zn(2+), which was confirmed by NMR spectroscopy. Previous studies indicate that the binding of Zn(2+) enhances calcium and target protein-binding affinities, which may contribute to its biological function. Thus, chemical shift perturbations observed here for residues in both EF-hand domains of S100B during Zn(2+) titrations could be detecting structural changes in the Ca(2+)-binding domains of S100B that are pertinent to its increase in Ca(2+)-binding affinity in the presence of Zn(2+). Furthermore, Zn(2+) binding causes helix 4 to extend by one full turn when compared to Ca(2+)-bound S100B. This change in secondary structure likely contributes to the increased binding affinity that S100B has for target peptides (i.e., TRTK peptide) in the presence of Zn(2+).




Molecular Function

  
Object Symbol
Species
Term
Qualifier
Evidence
With
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Original Reference(s)
S100bRatcalcium ion binding enablesIDA PMID:14621986UniProt 
S100bRatzinc ion binding enablesIDA PMID:14621986UniProt 


Genes (Rattus norvegicus)
S100b  (S100 calcium binding protein B)