The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference32 articles.
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4. Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli;Huang;J. Biol. Chem,1994
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1. Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes;Nature Communications;2024-08-03
2. Structural transitions in kinesin minus-end directed microtubule motility;2024-07-29
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4. Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules;Scientific Reports;2022-09-14
5. Interactions between motor domains in kinesin-14 Ncd — a molecular dynamics study;Biochemical Journal;2019-09-10
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