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. - Institut Pasteur Access content directly
Journal Articles Biomolecular NMR Assignments Year : 2009

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.

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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Dates and versions

pasteur-00460588 , version 1 (01-03-2010)

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Elouan Terrien, Catherine Simenel, Christophe Prehaud, Henri Prof Buc, Muriel Delepierre, 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.. Biomolecular NMR Assignments, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩. ⟨pasteur-00460588⟩

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