title: Kinesin Kar3 and Vik1 go head to head.
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.
authors: Department of Physics E22, Technical University Munich, Garching, Germany. guenther.woehlke@lrz.uni-muenchen.de
authors: Günther
authors: G
authors: Woehlke
authors: Manfred
authors: M
authors: Schliwa
mesh_terms: D000818:Animals; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; C063504:KAR3 protein, S cerevisiae; D008869:Microtubule-Associated Proteins; D029701:Saccharomyces cerevisiae Proteins; C119241:VIK1 protein, S cerevisiae; D016547:Kinesins