Informace o publikaci
19F Trp labelling as a selective probe into the dimeric interface
| Autoři | |
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| Rok publikování | 2022 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | The self-association of proteins is a fundamental mechanism in cell. The oligomerization offers a way of protein regulation, often broadening their functionality [1]. One of the rarest amino acids tryptophan (Trp) has a unique role in protein self-association [2]. It has been previously described that Trp is commonly present in so called dimerization hot spots partaking in dimer formation [3,4]. A method that could selectively focus on Trp could therefore offer a unique probe into protein dimerization. Nuclear magnetic resonance is a powerful tool in structural biology. Traditional double 13C, 15N labelling can be complemented by the 19F labelling which is a simple and straight-forward method [5]. The biggest advantage of 19F labelling is high signal intensity and a selective labelling of only chosen amino acid (usually Trp, Tyr or Phe), leading to less convoluted spectra without background noise. For these reasons, the 19F labelling may present a technique especially useful for determination of parameters connected to protein dimerization. In this work, we explore application of 19F Trp labelling on example of 14-3-3 proteins. The eukaryotic 14-3-3 proteins are important regulators involved in number of processes. Their dimeric form is crucial for proper function and the mechanism of dimer-ligand interaction has been thoroughly described [6]. Upon study of post-translational modifications, it has been discovered that phosphorylation of 14-3-3 at Ser58 located at dimeric interface leads to monomerization [7]. Intriguingly, residue neighbouring Ser58 is Trp59. We are thus comparing 19F Trp labelled dimeric 14-3-3 wild type and monomeric 14-3-3 phosphorylated at Ser58 and showing the possibilities that such labelling offers for study of dimerization. |
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