3kin
From Proteopedia
KINESIN (DIMERIC) FROM RATTUS NORVEGICUS
Overview
The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.
About this Structure
3KIN is a Protein complex structure of sequences from Rattus norvegicus. The following page contains interesting information on the relation of 3KIN with [Kinesin]. Full crystallographic information is available from OCA.
Reference
The crystal structure of dimeric kinesin and implications for microtubule-dependent motility., Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E, Cell. 1997 Dec 26;91(7):985-94. PMID:9428521 Page seeded by OCA on Sun May 4 22:05:07 2008
