ArticleNature1996
Crystal structure of the kinesin motor domain reveals a structural similarity to myosin.
Article in Nature, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 215 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
215 citing papers in PubMed, 644 citations in OpenAlex.
- A single-component optogenetic toolkit for reversible visualization and programmable control of microtubule dynamics.Cell reports methods · 2026Article
- Article
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail.Nature communications · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Maternal genetic variants in kinesin motor domains prematurely increase egg aneuploidy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- MARK2 phosphorylates KIF13A at a 14-3-3 binding site to polarize vesicular transport of transferrin receptor within dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- Interaction of Tau with Kinesin-1: Effect of Kinesin-1 Heavy Chain Elimination on Autophagy-Mediated Mutant Tau Degradation.Biomedicines · 2023Article
- Article
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- IFF: Identifying key residues in intrinsically disordered regions of proteins using machine learning.Protein science : a publication of the Protein Society · 2023Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- Tubulin Cytoskeleton in Neurodegenerative Diseases-not Only Primary Tubulinopathies.Cellular and molecular neurobiology · 2023Review
- Article
- Armadillo repeat-containing kinesin represents the versatile plus-end-directed transporter in Physcomitrella.Nature plants · 2023Article
- The tubulin structure, a quarter of a century later.Molecular biology of the cell · 2023Article
155 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin is the founding member of a superfamily of microtubule based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. It has two identical approximately 960-amino-acid chains containing an amino-terminal globular motor domain, a central alpha-helical region that enables dimer formation through a coiled-coil, and a carboxy-terminal tail domain that binds light chains and possibly an organelle receptor. The kinesin motor domain of approximately 340 amino acids, which can produce movement in vitro, is much smaller than that of myosin (approximately 850 amino acids) and dynein (1,000 amino acids), and is the smallest known molecular motor. Here, we report the crystal structure of the human kinesin motor domain with bound ADP determined to 1.8-A resolution by X-ray crystallography. The motor consists primarily of a single alpha/beta arrowhead-shaped domain with dimensions of 70 x 45 x 45 A. Unexpectedly, it has a striking structural similarity to the core of the catalytic domain of the actin-based motor myosin. Although kinesin and myosin have virtually no amino-acid sequence++ identity, and exhibit distinct enzymatic and motile properties, our results suggest that these two classes of mechanochemical enzymes evolved from a common ancestor and share a similar force-generating strategy.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.