Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7).
MAP7
MTBD
Microtubule-associated proteins
Microtubules
NMR resonance assignments
Journal
Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371
Informations de publication
Date de publication:
06 2023
06 2023
Historique:
received:
19
12
2022
accepted:
30
03
2023
medline:
2
6
2023
pubmed:
26
4
2023
entrez:
26
4
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37099260
doi: 10.1007/s12104-023-10124-8
pii: 10.1007/s12104-023-10124-8
pmc: PMC10232616
doi:
Substances chimiques
Kinesins
EC 3.6.4.4
Microtubule-Associated Proteins
0
MAP7 protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
83-88Informations de copyright
© 2023. The Author(s).
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