NMR paper Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

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[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

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11-24-2010, 10:01 PM

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Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

Biochemistry. 2004 Aug 17;43(32):10393-9

Authors: Lysek DA, Wüthrich K

Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified, although there are indications of a role in signal transduction in neurons. To gain further insight into the functional properties of cellular PrP, this paper investigated the binding of the C-terminal SH3 domain of the murine growth factor receptor-bound protein 2 (Grb2) to the murine PrP, using NMR, fluorescence, and circular dichroism spectroscopy. The SH3-binding site in murine PrP was thus found to be in the highly conserved region of residues 100-109, which contains prolines in positions 101 and 104. The protein-protein interaction, with a K(D) value of 5.5 microM, is abolished when either of these two prolines is replaced by leucine. In humans, two corresponding Pro --> Leu exchanges are found in patients who present with the Gerstmann-Sträussler-Scheinker syndrome. The results of the present study thus indicate a possible mechanism by which amino acid exchanges could influence a specific protein-protein interaction in a complex signal transduction cascade, which might be of functional significance in health and disease.

PMID: 15301538 [PubMed - indexed for MEDLINE]

Source: PubMed

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