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

被引：12

作者：

Terrien, Elouan ^{[1
]}

Simenel, Catherine ^{[1
]}

Prehaud, Christophe ^{[2
]}

Buc, Henri

Delepierre, Muriel ^{[1
]}

Lafon, Monique ^{[2
]}

Wolff, Nicolas ^{[1
]}

机构：

[1] Inst Pasteur, Dept Biol Struct & Chim, Unite Resonance Magnet Nucl Biomol, CNRS,URA 2185, F-75724 Paris 15, France

[2] Inst Pasteur, Dept Virol, Unite Neuroimmunol Virale, F-75724 Paris 15, France

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2009年 / 3卷 / 01期

关键词：

MAST205; NMR assignment; PDZ; Viral infection; DETERMINANT; DOMAIN;

D O I：

10.1007/s12104-008-9138-0

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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.

引用

页码：45 / 48

页数：4

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