Sandbox Reserved 957: Difference between revisions
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We study here the PDE5A catalytic fragment formed of amino acid residues from the 535th to the 860th [23]. In the inhibition, we talk about the Sildenafil mostly, because it's the most known (active ingredient in the Viagra®).<br \> | We study here the PDE5A catalytic fragment formed of amino acid residues from the 535th to the 860th [23]. In the inhibition, we talk about the Sildenafil mostly, because it's the most known (active ingredient in the Viagra®).<br \> | ||
== 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]. | ||
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The catalytic domain has 3 helical subdomains [24]:<br \> | The catalytic domain has 3 helical subdomains [24]:<br \> | ||
* 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),<scene name='60/604476/537_678/2'> from the 537th to the 678th residues</scene>.<br \> | * 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),<scene name='60/604476/537_678/2'> from the 537th to the 678th residues</scene>.<br \> | ||
* A linker domain: two antiparallels α9 and α10 helixes, and between a disordered region,from the 679th to the 725th residues.<br \> | * A linker domain: two antiparallels α9 and α10 helixes, and between a disordered region,<scene name='60/604476/679-725/1'>from the 679th to the 725th residues</scene>.<br \> | ||
* 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.<br \> | * 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),<scene name='60/604476/726-860/1'> from the 726th to the 860th residues</scene>.<br \> | ||
** α5, 6 and 8 surround α3 and form an interface with the linker domain and the CTD.<br \> | ** α5, 6 and 8 surround α3 and form an interface with the linker domain and the CTD.<br \> | ||