Evidence and sources

Measurements

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Big picture numbers

Structures

• 9BM0
  Human dynein-1 motor, primed

  Start of the power-stroke morph: the primed motor with a bent linker, at 2.8 Å. Same chain name and numbering as 9BM6 and 9BMH. Electron microscopy, 2.8 Å.
• 9BMH
  Human dynein-1 motor, ADP-vanadate

  Optional middle frame: the transition-state ring with the linker already straight but not yet docked. Electron microscopy, 2.8 Å.
• 9BM6
  Human dynein-1 motor, after the stroke

  End of the power-stroke morph. Same sample, buffer (5 mM ATP), chain name and numbering as 9BM0. Electron microscopy, 3.22 Å.
• 3VKG
  Dictyostelium dynein motor, 2.8 Å crystal

  The first high-resolution dynein motor. Use it for the atomic detail of the ring and its four nucleotide sites. X-ray diffraction, 2.81 Å.
• 4RH7
  Human dynein-2 motor, primed

  The crystal structure that first showed ring closure driving the linker into its primed shape. Dynein-2 drives intraflagellar transport. X-ray diffraction, 3.41 Å.
• 4AKG
  Yeast dynein motor

  The yeast motor used in most single-molecule stepping work, including the plus-end-directed stalk mutants. X-ray diffraction, 3.3 Å.
• 6RZB
  Dynein MTBD on a microtubule

  The foot of dynein on its track. Place it at the stalk tip, on the microtubule built for the kinesin scene. Electron microscopy, 4.1 Å.
• 5NUG
  Autoinhibited phi particle motors

  The switched-off dynein. Self-dimerized motors bind microtubules weakly until dynactin and an adaptor open them. Electron microscopy, 3.8 Å.
• 7Z8F
  Dynein-dynactin-BICDR transport complex

  The full transport machine: two dyneins on one dynactin with two adaptors. It is a 20 Å composite; the microtubule is not in the model. Over 100k atoms, so render one bead per residue. Electron microscopy, 20 Å.

References

1. 1Chai et al., Nat Struct Mol Biol 2025. The mechanochemical cycle of reactive full-length human dynein 1
2. 2Kon et al., Nature 2012. The 2.8 Å crystal structure of the dynein motor domain
3. 3Schmidt et al., Nature 2015. Structure of human cytoplasmic dynein-2 primed for its power stroke
4. 4Schmidt et al., Nat Struct Mol Biol 2012. Insights into dynein motor domain function from a 3.3-Å crystal structure
5. 5Zhang et al., Cell 2017. Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated
6. 6Lacey et al., eLife 2019. Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule
7. 7Chaaban et al., Nature 2022. Structure of dynein–dynactin on microtubules shows tandem adaptor binding
8. 8Burgess et al., Nature 2003. Dynein structure and power stroke
9. 9Roberts et al., Cell 2009. AAA+ Ring and Linker Swing Mechanism in the Dynein Motor
10. 10Reck-Peterson et al., Cell 2006. Single-Molecule Analysis of Dynein Processivity and Stepping Behavior
11. 11DeWitt et al., Science 2012. Cytoplasmic Dynein Moves Through Uncoordinated Stepping of the AAA+ Ring Domains
12. 12Qiu et al., Nat Struct Mol Biol 2012. Dynein achieves processive motion using both stochastic and coordinated stepping
13. 13Gennerich et al., Cell 2007. Force-Induced Bidirectional Stepping of Cytoplasmic Dynein
14. 14Mallik et al., Nature 2004. Cytoplasmic dynein functions as a gear in response to load
15. 15Can et al., Nature 2019. Directionality of dynein is controlled by the angle and length of its stalk
16. 16Huang et al., Cell 2012. Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor
17. 17Toropova et al., eLife 2014. Lis1 regulates dynein by sterically blocking its mechanochemical cycle
18. 18Htet et al., Nat Cell Biol 2020. LIS1 promotes the formation of activated cytoplasmic dynein-1 complexes
19. 19McKenney et al., Science 2014. Activation of cytoplasmic dynein motility by dynactin-cargo adapter complexes
20. 20Belyy et al., Nat Cell Biol 2016. The mammalian dynein–dynactin complex is a strong opponent to kinesin in a tug-of-war competition
21. 21Kon et al., Nat Struct Mol Biol 2009. Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
22. 22Gibbons et al., J Biol Chem 2005. The Affinity of the Dynein Microtubule-binding Domain Is Modulated by the Conformation of Its Coiled-coil Stalk
23. 23Carter et al., Science 2008. Structure and Functional Role of Dynein's Microtubule-Binding Domain
24. 24Urnavicius et al., Science 2015. The structure of the dynactin complex and its interaction with dynein
25. 25Urnavicius et al., Nature 2018. Cryo-EM shows how dynactin recruits two dyneins for faster movement
26. 26Wickstead et al., Traffic 2007. Dyneins Across Eukaryotes: A Comparative Genomic Analysis
27. 27Erzberger et al., Annu. Rev. Biophys. Biomol. Struct. 2006. EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS
28. 28Garbarino et al., BMC Genomics 2002. Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein
29. 29Furuta et al., Nat Nanotechnol 2017. Creating biomolecular motors based on dynein and actin-binding proteins
30. 30Ibusuki et al., Science 2022. Programmable molecular transport achieved by engineering protein motors to move on DNA nanotubes
31. 31Ton et al., Nat Struct Mol Biol 2023. Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport
32. 32UniProt Q14204, Cytoplasmic dynein 1 heavy chain 1 (human). Region annotations AAA1-AAA6 and stalk, by similarity