Michael Purol Sandbox 1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 13: | Line 13: | ||
==p19INK4d Structure== | ==p19INK4d Structure== | ||
The four INK4 proteins share a similar sturcture consisting of either four (p15 & p16) or five (p18 and '''p19''') ankyrin repeats (AR). | The four INK4 proteins share a similar sturcture consisting of either four (p15 & p16) or five (p18 and '''p19''') ankyrin repeats (AR). | ||
<scene name='Michael_Purol_Sandbox_1/Lys_62/1'>Lys 62</scene> | <scene name='Michael_Purol_Sandbox_1/Lys_62/1'>Lys 62</scene> | ||
| Line 22: | Line 22: | ||
==Cancer== | ==Cancer== | ||
In human osteosarcomas, p19INK4d has been found to phosphorylated at both Ser 66 and Ser 76, and also ubiquitinated at Lys 62. | |||
==Low et al. (2009) Study== | ==Low et al. (2009) Study== | ||
This study took an in-depth look at the structural consequences of phosphorylation at different sites of p19INK4d. Low et al. replaced Phe 86 with a trytophan residue which acted as a fluorescence-sensitive probe within a pseudo-wild type (in stability and function) mutant that displayed a hyperfluorescent intermediate which could be detected in unfolding and folding kinetics, but not at equilibrium conditions. | |||
Researchers then mimicked known phosphorylation sites with glutamate substitutions at <scene name='Michael_Purol_Sandbox_1/Ser_66/1'>Ser 66</scene> and <scene name='Michael_Purol_Sandbox_1/Ser_76/1'>Ser 76</scene> within ''E. coli'' to test the impact of introduced negative charges at these positions on the structural stability of P19INK4d. | |||
==Ceruti et al. (2005) Study== | ==Ceruti et al. (2005) Study== | ||