3KIN

KINESIN (DIMERIC) FROM RATTUS NORVEGICUS

Summary for 3KIN

• Entry DOI: 10.2210/pdb3kin/pdb
• Descriptor: KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: motor protein, cytoskeleton
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 4
• Total formula weight: 81496.62

Authors

Kozielski, F.,Sack, S.,Marx, A.,Thormahlen, M.,Schonbrunn, E.,Biou, V.,Thompson, A.,Mandelkow, E.-M.,Mandelkow, E. (deposition date: 1997-08-25, release date: 1998-10-14, Last modification date: 2024-12-25)

Primary citation

Kozielski, F.,Sack, S.,Marx, A.,Thormahlen, M.,Schonbrunn, E.,Biou, V.,Thompson, A.,Mandelkow, E.M.,Mandelkow, E.
The crystal structure of dimeric kinesin and implications for microtubule-dependent motility.
Cell(Cambridge,Mass.), 91:985-994, 1997

PubMed Abstract: 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.

PubMed: 9428521
DOI: 10.1016/S0092-8674(00)80489-4

Experimental method

X-RAY DIFFRACTION (3.1 Å)