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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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https://hal-pasteur.archives-ouvertes.fr/pasteur-00460588
Contributor : Mireille Gau <>
Submitted on : Monday, March 1, 2010 - 4:48:31 PM
Last modification on : Tuesday, July 7, 2020 - 9:26:28 AM

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Elouan Terrien, Catherine Simenel, Christophe Prehaud, Henri 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, Springer, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩. ⟨pasteur-00460588⟩

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