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The microtubule-associated protein 7 (MAP7) is a protein involved in cargo transport along microtubules (MTs) by interacting with kinesin-1 through the C-terminal kinesin-binding domain. Moreover, the protein is reported to stabilize MT, thereby playing a key role in axonal branch development. An important element for this latter function is the 112 amino-acid long N-terminal microtubule-binding domain (MTBD) of MAP7. Here we report NMR backbone and side-chain assignments that suggest a primarily alpha-helical secondary fold of this MTBD in solution. The MTBD contains a central long α-helical segment that includes a short four-residue 'hinge' sequence with decreased helicity and increased flexibility. Our data represent a first step towards analysing the complex interaction of MAP7 with MTs at an atomic level via NMR spectroscopy. © 2023. The Author(s).

Citation

Agnes Adler, Lenette F Kjaer, J Wouter Beugelink, Marc Baldus, Hugo van Ingen. Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7). Biomolecular NMR assignments. 2023 Jun;17(1):83-88

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PMID: 37099260

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