ArticleNature communications2017
Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Advancing Cancer Therapy: The Role of KIF20A as a Target for Inhibitor Development and Immunotherapy.Cancers · 2024Review
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- Article
- Mechanistic insights into central spindle assembly mediated by the centralspindlin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural snapshots of the kinesin-2 OSM-3 along its nucleotide cycle: implications for the ATP hydrolysis mechanism.FEBS open bio · 2021Article
- CYK4 relaxes the bias in the off-axis motion by MKLP1 kinesin-6.Communications biology · 2021Article
- Insights into Kinesin-1 Stepping from Simulations and Tracking of Gold Nanoparticle-Labeled Motors.Biophysical journal · 2019Article
- Single-molecule in vitro reconstitution assay for kinesin-1-driven membrane dynamics.Biophysical reviews · 2019Review
- The Orphan Kinesin PAKRP2 Achieves Processive Motility via a Noncanonical Stepping Mechanism.Biophysical journal · 2019Article
- Biophysical nanotools for single-molecule dynamics.Biophysical reviews · 2018Review
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Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Kinesins hydrolyse ATP to transport intracellular cargoes along microtubules. Kinesin neck linker (NL) functions as the central mechano-chemical coupling element by changing its conformation through the ATPase cycle. Here we report the crystal structure of kinesin-6 Zen4 in a nucleotide-free, apo state, with the NL initial segment (NIS) adopting a backward-docked conformation and the preceding α6 helix partially melted. Single-molecule fluorescence resonance energy transfer (smFRET) analyses indicate the NIS of kinesin-1 undergoes similar conformational changes under tension in the two-head bound (2HB) state, whereas it is largely disordered without tension. The backward-docked structure of NIS is essential for motility of the motor. Our findings reveal a key missing conformation of kinesins, which provides the structural basis of the stable 2HB state and offers a tension-based rationale for an optimal NL length to ensure processivity of the motor.
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