Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain

被引:2
|
作者
Orban-Nemeth, Zsuzsanna [1 ]
Henen, Morkos A. [2 ]
Geist, Leonhard [2 ]
Zerko, Szymon [3 ]
Saxena, Saurabh [3 ]
Stanek, Jan [3 ]
Kozminski, Wiktor [3 ]
Propst, Friedrich [1 ]
Konrat, Robert [2 ]
机构
[1] Univ Vienna, Dept Biochem & Cell Biol, Max F Perutz Labs, A-1030 Vienna, Austria
[2] Univ Vienna, Dept Struct & Computat Biol, Max F Perutz Labs, A-1030 Vienna, Austria
[3] Univ Warsaw, Fac Chem, PL-02093 Warsaw, Poland
基金
奥地利科学基金会;
关键词
Microtubule-associated protein; Microtubule binding domain; Random sampling; Intrinsically disordered protein; PROTEIN 1B MAP1B; RESONANCE ASSIGNMENT; NERVOUS-SYSTEM; MICE; GENE; 1A;
D O I
10.1007/s12104-013-9466-6
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Microtubule-associated protein 1B (MAP1B) is a classical high molecular mass microtubule-associated protein expressed at high levels in the brain. It confers specific properties to neuronal microtubules and is essential for neuronal differentiation, brain development and synapse maturation. Misexpression of the protein contributes to the development of brain disorders in humans. However, despite numerous reports demonstrating the importance of MAP1B in regulation of the neuronal cytoskeleton during neurite extension and axon guidance, its mechanism of action is still elusive. Here we focus on the intrinsically disordered microtubule binding domain of the light chain of MAP1B. In order to obtain more detailed structural information about this domain we assigned NMR chemical shifts of backbone and aliphatic side chain atoms.
引用
收藏
页码:123 / 127
页数:5
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