Journal Article

PUBDB-2017-09758

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structures of kinesin and kinesin–microtubule interactions

Mandelkow, E. (Corresponding author)MPG* ; Hoenger, A. (Corresponding author)

1999
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/S0955-0674(99)80005-2

Abstract: 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.

Note: F-Bereich; Max-Planck-Gesellschaft

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Contributing Institute(s):

1. DESY Retrocat (DESY(-2012))

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. No specific instrument

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Database coverage:
; BIOSIS Previews ; BIOSIS Reviews Reports And Meetings ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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