Abstract
Most of microbes hijack the cellular machinery to their advantage by interacting with specific target of the host cell. Glycoprotein of rabies virus is a key factor controlling the homeostasis of infected neuronal cells and proteins belonging to the human microtubule associated serine threonine kinase family have been identified as potential cellular partners. As a first step towards its structural study, we have assigned the backbone and side chain nuclei resonances of the PDZ domain (PSD-95, Discs Large, ZO-1) of MAST205 in complex with the C-terminal residues of the glycoprotein of rabies virus. The BMRB accession code is 155972.
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Acknowledgements
We thanks J. D’Alayer from Institut Pasteur Facility “Analyse et Microséquençage des Protéines” for mass spectrometry and microsequencing and V. Bondet, E. Frachon and J. Bellalou from Institut Pasteur Facility “Production de Protéines recombinantes et d’Anticorps” for protein expression and purification. This work was supported by the Agence Nationale de la Recherche (ANR-MIME Patho-PDZ). E. Terrien is recipient of a MRT fellowship.
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Terrien, E., Simenel, C., Prehaud, C. et al. 1H, 13C and 15N resonance assignments of the PDZ of microtubule-associated serine/threonine kinase 205 (MAST205) in complex with the C-terminal motif from the rabies virus glycoprotein. Biomol NMR Assign 3, 45–48 (2009). https://doi.org/10.1007/s12104-008-9138-0
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DOI: https://doi.org/10.1007/s12104-008-9138-0