Interaction of kinesin motors, microtubules, and MAPs.
Kinesins are a family of microtubule-dependent motor proteins that carry cargoes such as vesicles, organelles, or protein complexes along microtubules. Here we summarize structural studies of the "conventional" motor protein kinesin-1 and its interactions with microtubules, as determined by X-ray crystallography and cryo-electron microscopy. In particular, we consider the docking between the kinesin motor domain and tubulin subunits and summarize the evidence that kinesin binds mainly to beta tubulin with the switch-2 helix close to the intradimer interface between alpha and beta tubulin.
Marx
A
A
Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, 22607, Hamburg, Germany.
Müller
J
J
Mandelkow
E-M
EM
Hoenger
A
A
Mandelkow
E
E
D000818:Animals; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D016547:Kinesins; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism*; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism*
D008869:Microtubule-Associated Proteins; D021122:Protein Subunits; D014404:Tubulin; D016547:Kinesins