Author:
Adler Agnes,Kjaer Lenette F.,Beugelink J. Wouter,Baldus Marc,van Ingen Hugo
Abstract
AbstractThe 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.
Funder
Nederlandse Organisatie voor Wetenschappelijk Onderzoek
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Cited by
3 articles.
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