Kinesin Kar3 and Vik1 Go Head to Head.
From: Department of Physics E22, Technical University Munich, Garching, Germany. guenther.woehlke@lrz.uni-muenchen.de
Cell
- Publish Date: Mar 2007
- ISSN: 0092-8674
- Volume: 128
- Issue: 6
- Pages: 1033-4
- Medium: Print
- Language: English
- Citation (JAMA): Woehlke Günther, Schliwa Manfred, et al. Kinesin Kar3 and Vik1 Go Head to Head.. Cell Mar 2007;128:1033-4
Abstract
The yeast kinesin motor protein Kar3 forms a heterodimer with a nonmotor protein Vik1. A study in this issue by Allingham et al. (2007) reveals that Vik1 unexpectedly has a structure similar to a kinesin motor domain yet lacks a nucleotide-binding site and is thus catalytically inactive. However, this does not hinder movement of the heterodimer because other features of the remarkably divergent Vik1 motor domain are retained, including the ability to bind microtubules.
Mesh Headings (Keywords): Animals, Fungal Proteins, Kinesin, Microtubule-Associated Proteins, Microtubules, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17382876
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