Backbone and side-chain ^sup 1^H, ^sup 15^N and ^sup 13^C resonance assignments of the microtubule-binding domain of yeast cytoplasmic dynein in the high and low-affinity states

Cytoplasmic dynein is a motor protein that walks toward the minus end of microtubules (MTs) by utilizing the energy of ATP hydrolysis. The heavy chain of cytoplasmic dynein contains the microtubule-binding domain (MTBD). Switching of MTBD between high and low affinity states for MTs is crucial for p...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2014-10, Vol.8 (2), p.379
Main Authors: Takarada, Osamu, Nishida, Noritaka, Kikkawa, Masahide, Shimada, Ichio
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Cytoplasm
NMR
Nuclear magnetic resonance
Proteins
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Summary:Cytoplasmic dynein is a motor protein that walks toward the minus end of microtubules (MTs) by utilizing the energy of ATP hydrolysis. The heavy chain of cytoplasmic dynein contains the microtubule-binding domain (MTBD). Switching of MTBD between high and low affinity states for MTs is crucial for processive movement of cytoplasmic dynein. Previous biochemical studies demonstrated that the affinity of MTBD is regulated by the AAA+ family ATPase domain, which is separated by 15 nm long coiled-coil helix. In order to elucidate the structural basis of the affinity switching mechanism of MTBD, we designed two MTBD constructs, termed MTBD-High and MTBD-Low, which are locked in high and low affinity state for MTs, respectively, by introducing a disulfide bond between the coiled-coil helix. Here, we established the backbone and side-chain assignments of MTBD-High and MTBD-Low for further structural analyses. [PUBLICATION ABSTRACT]
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-013-9522-2