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Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7).

ABSTRACT: 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.

SUBMITTER: Adler A

PROVIDER: S-EPMC10232616 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature

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Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7).

Adler Agnes A Kjaer Lenette F LF Beugelink J Wouter JW Baldus Marc M van Ingen Hugo H

Biomolecular NMR assignments 20230426 1

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 primaril ...[more]

PMID: 37099260

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