UNDERSTANDING THE MECHANISM OF MOTILITY OF THE HETERODIMERIC KINESIN-14 KAR3VIK1
The kinesin-14 Kar3 from Saccharomyces cerevisiae (Sc) is a C-terminal motor that forms a heterodimer with the kinesin-accessory protein Vik1. Although Vik1 possesses a typical kinesin motor domain (MD) fold, it lacks a nucleotide-binding site. However, it binds microtubules with affinities that can...
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| Language: | en en |
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2013
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| Online Access: | http://hdl.handle.net/1974/8118 |