Journal Article

PHPPUBDB-3017

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Interaction of kinesin motors, microtubules, and MAPs

Marx, A. ; Müller, J. ; Mandelkow, E.-M. ; Hoenger, A. ; Mandelkow, E. ; DESY

2006
Springer Science + Business Media B.V Dordrecht [u.a.]

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Please use a persistent id in citations: doi:10.1007/s10974-005-9051-4

Abstract: 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.

Keyword(s): Animals (MeSH) ; Crystallography, X-Ray: methods (MeSH) ; Humans (MeSH) ; Kinesin (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: metabolism (MeSH) ; Microtubules: metabolism (MeSH) ; Microtubules: ultrastructure (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Secondary (MeSH) ; Protein Structure, Tertiary (MeSH) ; Protein Subunits: chemistry (MeSH) ; Protein Subunits: metabolism (MeSH) ; Tubulin: chemistry (MeSH) ; Tubulin: metabolism (MeSH) ; Microtubule-Associated Proteins ; Protein Subunits ; Tubulin ; Kinesin

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Contributing Institute(s):

1. Max-Planck-Arbeitsgruppen (MPG)

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2006
Notes: MPG beamline BW6 No copyright permission for full text

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Database coverage:
; JCR ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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