Sandbox Reserved 708
From Proteopedia
(Difference between revisions)
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The Tau protein possesses <scene name='Sandbox_Reserved_708/Mg_ions/2'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/2'>two molecules of ADP</scene>(Adenosine DiPhosphate) | The Tau protein possesses <scene name='Sandbox_Reserved_708/Mg_ions/2'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/2'>two molecules of ADP</scene>(Adenosine DiPhosphate) | ||
This enzyme is activated by phosphorylation at <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/2'>Tyr-216</scene> and inactivated by phosphorylation at Ser-9 (not shown here because this structure start at residue 35). | This enzyme is activated by phosphorylation at <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/2'>Tyr-216</scene> and inactivated by phosphorylation at Ser-9 (not shown here because this structure start at residue 35). | ||
| - | This structure possesses 12 hydrogen bonds in order to stabilize the molecule, but in this case only three are shown (with red dashed lines) with there <scene name='Sandbox_Reserved_708/Hbonds_amino_acids/ | + | This structure possesses 12 hydrogen bonds in order to stabilize the molecule, but in this case only three are shown (with red dashed lines) with there <scene name='Sandbox_Reserved_708/Hbonds_amino_acids/4'>amino acids (17)</scene> engaged |
== External Ressources == | == External Ressources == | ||
== References == | == References == | ||
Revision as of 20:21, 30 December 2012
Contents |
Descritpion
Activity
at tyrosine-216 in GSK-3β or tyrosine-279 in GSK-3α enhances the enzymatic activity of GSK-3, while phosphorlyation of serine-9 in GSK-3β or serine-21 in GSK-3α significantly decreases active site availability
Structure
These are the engaged in the catalytic site of the protein, they are polar and localised in 3' end (Asp-181, Lys-183, Gln-185, Asn-186 and Ser-219. The Tau protein possesses as well as (Adenosine DiPhosphate) This enzyme is activated by phosphorylation at and inactivated by phosphorylation at Ser-9 (not shown here because this structure start at residue 35). This structure possesses 12 hydrogen bonds in order to stabilize the molecule, but in this case only three are shown (with red dashed lines) with there engaged
