首页 | 本学科首页   官方微博 | 高级检索  
     


Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain
Authors:Zsuzsanna Orbán-Németh  Morkos A. Henen  Leonhard Geist  Szymon Żerko  Saurabh Saxena  Jan Stanek  Wiktor Koźmiński  Friedrich Propst  Robert Konrat
Affiliation:1. Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter Campus 1, 1030, Vienna, Austria
2. Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter Campus 5, 1030, Vienna, Austria
3. Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093, Warsaw, Poland
Abstract: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.
Keywords:
本文献已被 SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号