Sandbox Reserved 957: Difference between revisions
No edit summary |
No edit summary |
||
| Line 12: | Line 12: | ||
== Structure of catalytic site == | == Structure of catalytic site == | ||
The only catalytic fragment is effective, so the regulations sites and the dimerization to a trimeric enzyme are useless for the catalytic activity. Moreover, this catalytic moiety has the same activity that the wild-type enzyme, so maybe the enzyme is monomeric in the cell [24]. | The only catalytic fragment is effective, so the regulations sites and the dimerization to a trimeric enzyme are useless for the catalytic activity. Moreover, this catalytic moiety has the same activity that the wild-type enzyme, so maybe the enzyme is monomeric in the cell [24]. | ||
Catalytic domain is conserved for the PDE family, between 20% and 40%, and the variant reactions of the PDE inhibitors on the different PDEs may be caused by the more variant regulatory sites [25]. | Catalytic domain is conserved for the PDE family, between 20% and 40%, and the variant reactions of the PDE inhibitors on the different PDEs may be caused by the more variant regulatory sites [25]./n | ||
The catalytic domain has 3 helical subdomains [24]: | The catalytic domain has 3 helical subdomains [24]:/n | ||
- A N-terminal cyclin-fold region with eight helixes [26]: 5 α-helixes (1, 3, 5, 6 and 8) and 3 310-helixes (2,4, and 7), from the 537th to the 678th residues. | - A N-terminal cyclin-fold region with eight helixes [26]: 5 α-helixes (1, 3, 5, 6 and 8) and 3 310-helixes (2,4, and 7), from the 537th to the 678th residues./n | ||
- A linker domain: two antiparallels α9 and α10 helixes, and between a disordered region, from the 679th to the 725th residues. | - A linker domain: two antiparallels α9 and α10 helixes, and between a disordered region, from the 679th to the 725th residues. | ||
- A C-terminal buddle pocket with eight helixes: 5 long α-helixes (11, 12, 14, 17 and 18) and 3 smaller helixes (13, 15 and 16), from the 726th to the 860th residues. | - A C-terminal buddle pocket with eight helixes: 5 long α-helixes (11, 12, 14, 17 and 18) and 3 smaller helixes (13, 15 and 16), from the 726th to the 860th residues. | ||