3kin
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(New page: 200px<br /> <applet load="3kin" size="450" color="white" frame="true" align="right" spinBox="true" caption="3kin, resolution 3.1Å" /> '''KINESIN (DIMERIC) FR...)
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Revision as of 07:03, 18 November 2007
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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 with ADP as ligand. 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 Nov 18 09:10:29 2007
