Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain |
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Authors: | Zsuzsanna Orbán-Németh Morkos A. Henen Leonhard Geist Szymon Żerko Saurabh Saxena Jan Stanek Wiktor Koźmiński Friedrich Propst Robert Konrat |
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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
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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. |
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