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Structures of kinesin and kinesin-microtubule interactions
Structures of kinesin and kinesin-microtubule interactions.
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Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution ( approximately 0.2-0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer. In addition, cryo-electron microscopy and image reconstruction have revealed microtubules decorated with kinesin at intermediate resolution ( approximately 2 nm), showing the distribution and orientation of kinesin heads on the microtubule surface. The comparison of the X-ray and electron microscopy results yields a model of how monomeric motor domains bind to the microtubule but the binding of dimeric motors, their stoichiometry, or the influence of nucleotides remains a matter of debate.
Mandelkow E, Hoenger A
Current opinion in cell biology
1999-02-01 00:00
11
1
34-44
Animals,Brain,Cryoelectron Microscopy,Crystallography, X-Ray,Drosophila Proteins,Drosophila melanogaster,Humans,Kinesin,Kinetics,Microtubules,Models, Molecular,Protein Conformation,Rats,Structure-Activity Relationship,Drosophila Proteins,ncd protein, Drosophila,Kinesin
Max-Planck-Unit for Structural Molecular Biology Notkestrasse 85 D-22607 Hamburg Germany mandmpasmbdesyde
Curr. Opin. Cell Biol.
0955-0674
S0955-0674(99)80005-2
575
True
10047529
