Kinesin-like protein KIF2C is a
protein that in humans is encoded by the KIF2Cgene.[5][6]
The protein encoded by this gene is a member of
kinesin-like protein family, and contains common ATPase site structures such as the P-loop, Switch 1, and Switch 2.[7] Most proteins of this family are
microtubule-dependent
molecular motors that transport
organelles within cells and move
chromosomes during
cell division. This protein acts to regulate microtubule dynamics in cells and is important for
anaphasechromosome segregation and may be required to coordinate the onset of sister
centromere separation.[6]
A ribbon and surface diagram of the KIF2C motor domain.[8] The kinesin structure is pseudo-colored to highlight the ATPase site with a bound nucleotide. The figure then presents KIF2C binding to the tubulin dimer and finally visualizes a KIF2C motor head in the context of the microtubule filament.
Wordeman L, Wagenbach M, Maney T (2000). "Mutations in the ATP-binding domain affect the subcellular distribution of mitotic centromere-associated kinesin (MCAK)". Cell Biology International. 23 (4): 275–286.
doi:
10.1006/cbir.1999.0359.
PMID10600236.
S2CID29403722.
Sun Y, Huang YC, Xu QZ, Wang HP, Bai B, Sui JL, Zhou PK (July 2006). "HIV-1 Tat depresses DNA-PK(CS) expression and DNA repair, and sensitizes cells to ionizing radiation". International Journal of Radiation Oncology, Biology, Physics. 65 (3): 842–850.
doi:
10.1016/j.ijrobp.2006.02.040.
PMID16751065.
Kinesin-like protein KIF2C is a
protein that in humans is encoded by the KIF2Cgene.[5][6]
The protein encoded by this gene is a member of
kinesin-like protein family, and contains common ATPase site structures such as the P-loop, Switch 1, and Switch 2.[7] Most proteins of this family are
microtubule-dependent
molecular motors that transport
organelles within cells and move
chromosomes during
cell division. This protein acts to regulate microtubule dynamics in cells and is important for
anaphasechromosome segregation and may be required to coordinate the onset of sister
centromere separation.[6]
A ribbon and surface diagram of the KIF2C motor domain.[8] The kinesin structure is pseudo-colored to highlight the ATPase site with a bound nucleotide. The figure then presents KIF2C binding to the tubulin dimer and finally visualizes a KIF2C motor head in the context of the microtubule filament.
Wordeman L, Wagenbach M, Maney T (2000). "Mutations in the ATP-binding domain affect the subcellular distribution of mitotic centromere-associated kinesin (MCAK)". Cell Biology International. 23 (4): 275–286.
doi:
10.1006/cbir.1999.0359.
PMID10600236.
S2CID29403722.
Sun Y, Huang YC, Xu QZ, Wang HP, Bai B, Sui JL, Zhou PK (July 2006). "HIV-1 Tat depresses DNA-PK(CS) expression and DNA repair, and sensitizes cells to ionizing radiation". International Journal of Radiation Oncology, Biology, Physics. 65 (3): 842–850.
doi:
10.1016/j.ijrobp.2006.02.040.
PMID16751065.