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8FDT

Engineered human dynein motor domain in the microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi

Summary for 8FDT
Entry DOI10.2210/pdb8fdt/pdb
EMDB information29012
DescriptorCytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase, Platelet-activating factor acetylhydrolase IB subunit beta, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
Functional Keywordsdynein, motor domain, microtubule-unbound, motor protein, lis1
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight492209.94
Authors
Ton, W.,Wang, Y.,Chai, P. (deposition date: 2022-12-04, release date: 2023-06-21, Last modification date: 2023-11-15)
Primary citationTon, W.D.,Wang, Y.,Chai, P.,Beauchamp-Perez, C.,Flint, N.T.,Lammers, L.G.,Xiong, H.,Zhang, K.,Markus, S.M.
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.
Nat.Struct.Mol.Biol., 30:1365-1379, 2023
Cited by
PubMed: 37322240
DOI: 10.1038/s41594-023-01010-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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