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.

Elouan Terrien (1) , Catherine Simenel (1) , Christophe Prehaud (2) , Henri Prof Buc (3) , Muriel Delepierre (1) , Monique Lafon (2) , Nicolas Wolff (1)

1 Résonance Magnétique Nucléaire des Biomolécules
2 Neuro-Immunologie Virale
3 Institut Pasteur [Paris]

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.

Domains: Life Sciences [q-bio]; Microbiology and Parasitology

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⟩