Structures of kinesin and kinesin-microtubule interactions.
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.
Max-Planck-Unit for Structural Molecular Biology Notkestrasse 85 D-22607 Hamburg Germany. mand@mpasmb.desy.de
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Mandelkow
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Hoenger
D000818:Animals; D001921:Brain / Q000378:metabolism / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000737:chemistry; D006801:Humans; D016547:Kinesins / Q000737:chemistry*; D007700:Kinetics; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats; D013329:Structure-Activity Relationship
D029721:Drosophila Proteins; C066696:ncd protein, Drosophila; D016547:Kinesins