4BN2

The crystal structure of kinesin-like protein KIF15

4BN2 の概要

• エントリーDOI: 10.2210/pdb4bn2/pdb
• 分子名称: KINESIN-LIKE PROTEIN KIF15, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: motor protein, kinesin, motor domain
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 119477.54

構造登録者

Klejnot, M.,Falnikar, A.,Ulaganathan, V.,Cross, R.,Baas, P.,Kozielski, F. (登録日: 2013-05-13, 公開日: 2014-01-15, 最終更新日: 2024-11-13)

主引用文献

Klejnot, M.,Falnikar, A.,Ulaganathan, V.,Cross, R.A.,Baas, P.W.,Kozielski, F.
The Crystal Structure and Biochemical Characterization of Kif15: A Bifunctional Molecular Motor Involved in Bipolar Spindle Formation and Neuronal Development
Acta Crystallogr.,Sect.D, 70:123-, 2014

PubMed Abstract: Kinesins constitute a superfamily of microtubule-based motor proteins with important cellular functions ranging from intracellular transport to cell division. Some kinesin family members function during the mitotic phase of the eukaryotic cell cycle and are crucial for the successful progression of cell division. In the early stages of mitosis, during prometaphase, certain kinesins are required for the formation of the bipolar spindle, such as Eg5 and Kif15, which seem to possess partially overlapping functions. Because kinesins transform the chemical energy from ATP hydrolysis into mechanical work, inhibition of their function is a tractable approach for drug development. Drugs targeting Eg5 have shown promise as anticancer agents. Kif15 has recently come to the fore because it can substitute the functions of Eg5, and may itself have potential as a prospective drug target. Here, the initial biochemical, kinetic and structural characterization of Kif15 is reported and it is compared with the functionally related motor Eg5. Although Kif15 contains ADP in the catalytic site, its motor-domain structure was captured in the `ATP-like' configuration, with the neck linker docked to the catalytic core. The interaction of Kif15 with microtubules was also investigated and structural differences between these two motors were elucidated which indicate profound differences in their mode of action, in agreement with current models of microtubule cross-linking and sliding.

PubMed: 24419385
DOI: 10.1107/S1399004713028721

実験手法

X-RAY DIFFRACTION (2.695 Å)