Preliminary crystallization studies of calmodulin-dependent protein phosphatase (calcineurin) from bovine brain
- Cite this article as:
- Balendiran, K., Tan, Y., Sharma, R.K. et al. Mol Cell Biochem (1995) 149: 127. doi:10.1007/BF01076570
Calcineurin is a serine/threonine protein phosphatase which catalyzes the hydrolysis of both phosphoseryl/phosphothreonyl and phosphotyrosyl proteins as well as low molecular weight compounds such as p-nitrophenyl phosphate. It is a hetero-dimeric protein consisting of a 60 kDa A chain and 19 kDa B chain. Calcineurin A is organized into functionally distinct domains such as a catalytic domain, a calcineurin B binding domain, a calmodulin-binding domain, and an inhibitory domain. Calcineurin B has four EF-hand calcium binding domains with a secondary structure that is homologous to calmodulin but its metal binding properties are more similar to troponin-C. The N-terminal myristoyl group of calcineurin B might play a role in the interaction between subunits A and B during phosphorylation/dephosphorylation processes. Crystals of size 0.125×0.07×0.03 mm and 0.7×0.03×0.02 mm have been obtained for calcineurin and the A subunit respectively. Crystals of calcineurin show strong diffraction to 5.3 Å and weak diffraction to 3.0 Å on rotating anode operated at 50 kV and 100 mA. Further work is in progress to improve the X-ray diffraction quality of these crystals and to obtain well diffracting crystals of calcineurin B.