2kin

From Proteopedia

Revision as of 13:27, 23 March 2008

KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS

Overview

We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550-554]. Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure.

About this Structure

2KIN is a Protein complex structure of sequences from Rattus norvegicus. The following page contains interesting information on the relation of 2KIN with [Kinesin]. Full crystallographic information is available from OCA.

Reference

X-ray structure of motor and neck domains from rat brain kinesin., Sack S, Muller J, Marx A, Thormahlen M, Mandelkow EM, Brady ST, Mandelkow E, Biochemistry. 1997 Dec 23;36(51):16155-65. PMID:9405049

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