Sandbox Reserved 708: Difference between revisions
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This complex is composed by two subunits A (green) and B (blue) linked by 12 hydrogen bonds in order to stabilize the molecule. But in this case only four are shown (with red dashed lines) with there <scene name='Sandbox_Reserved_708/Hbonds_amino_acids/7'>amino acids (17)</scene> engaged: Ser-66, Ser-215,Tyr-216, Arg-220, Gly-230, Asp-260, Gly-262, Val-263, Tyr-288, Ser-715,Tyr-716, Arg-720, Asp-760,Val-763, Asp-764, Tyr-788 and Glu-790. | This complex is composed by two subunits A (green) and B (blue) linked by 12 hydrogen bonds in order to stabilize the molecule. But in this case only four are shown (with red dashed lines) with there <scene name='Sandbox_Reserved_708/Hbonds_amino_acids/7'>amino acids (17)</scene> engaged: Ser-66, Ser-215,Tyr-216, Arg-220, Gly-230, Asp-260, Gly-262, Val-263, Tyr-288, Ser-715,Tyr-716, Arg-720, Asp-760,Val-763, Asp-764, Tyr-788 and Glu-790. | ||
This structure also possesses <scene name='Sandbox_Reserved_708/Mg_ions/3'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/3'>two molecules of ADP</scene>(Adenosine DiPhosphate). | This structure also possesses <scene name='Sandbox_Reserved_708/Mg_ions/3'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/3'>two molecules of ADP</scene>(Adenosine DiPhosphate).Arg-141 is one of the key residues for <scene name='Sandbox_Reserved_708/Adp_recognition_by_arg141/1'>specific ATP/ADP recognition</scene> by GSK3. | ||
These are the <scene name='Sandbox_Reserved_708/Catalytic_site/7'>amino acids</scene> 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 | These are the <scene name='Sandbox_Reserved_708/Catalytic_site/7'>amino acids</scene> 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. | ||
This enzyme is activated by phosphorylation on <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/3'>Tyr-216</scene> and inactivated by phosphorylation on Ser-9 (not shown here because this structure start at residue 35). But the phosphorylation on Tyr-216 is not mandatory for the activity,<ref>"Crystal Structure of Glycogen Synthase Kinase 3β: Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition" Rana Dajani, Elizabeth Fraser, S. Mark Roe, Neville Young, Valerie Good, Trevor C. Dale and Laurence H. Pearl1; Cell, Vol. 105, 721–732, June 15, 2001, Copyright 2001 by Cell Press</ref>. | This enzyme is activated by phosphorylation on <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/3'>Tyr-216</scene> and inactivated by phosphorylation on Ser-9 (not shown here because this structure start at residue 35). But the phosphorylation on Tyr-216 is not mandatory for the activity,<ref>"Crystal Structure of Glycogen Synthase Kinase 3β: Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition" Rana Dajani, Elizabeth Fraser, S. Mark Roe, Neville Young, Valerie Good, Trevor C. Dale and Laurence H. Pearl1; Cell, Vol. 105, 721–732, June 15, 2001, Copyright 2001 by Cell Press</ref>. | ||