TY  - JOUR
AU  - Mandelkow, Eckhard
AU  - Hoenger, Andreas
TI  - Structures of kinesin and kinesin–microtubule interactions
JO  - Current opinion in cell biology
VL  - 11
IS  - 1
SN  - 0955-0674
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PUBDB-2017-09758
SP  - 34 - 44
PY  - 1999
N1  - F-Bereich; Max-Planck-Gesellschaft
AB  - Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution (∼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 (∼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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000078614000004
C6  - pmid:10047529
DO  - DOI:10.1016/S0955-0674(99)80005-2
UR  - https://bib-pubdb1.desy.de/record/390701
ER  -