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. - Archive ouverte HAL 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.

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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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