Sandbox Reserved 708: Difference between revisions
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== Description == | == Description == | ||
The Glycogen Synthase Kinase 3 beta- GSK-3β, also known as the tau protein kinase I, is a serine protein kinase that participates in many different pathways regulating critical cellular functions as structure, gene expression, mobility, and apoptosis,<ref> | The Glycogen Synthase Kinase 3 beta- GSK-3β, also known as the tau protein kinase I, is a serine protein kinase that participates in many different pathways regulating critical cellular functions as structure, gene expression, mobility, and apoptosis,<ref name="SINR"> "Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta." | ||
Aoki, M., Yokota, T., Sugiura, I., Sasaki, C., Hasegawa, T., Okumura, C., Ishiguro, K., Kohno, T., Sugio, S., Matsuzaki, T. | Aoki, M., Yokota, T., Sugiura, I., Sasaki, C., Hasegawa, T., Okumura, C., Ishiguro, K., Kohno, T., Sugio, S., Matsuzaki, T. | ||
Journal: (2004) Acta Crystallogr.,Sect.D60: 439-446</ref>. GSK-3 phosphorylates a large number of substrates and is himself regulated by phosphorylation,<ref name="GSK3 IDT"> "Glycogen Synthase Kinase-3 (GSK3): Inflammation, Diseases, and Therapeutics." Richard S. Jope,* Christopher J. Yuskaitis, and Eléonore Beurel Neurochem Res. 2007; 32(4-5): 577-595.</ref>. | Journal: (2004) Acta Crystallogr.,Sect.D60: 439-446</ref>. GSK-3 phosphorylates a large number of substrates and is himself regulated by phosphorylation,<ref name="GSK3 IDT"> "Glycogen Synthase Kinase-3 (GSK3): Inflammation, Diseases, and Therapeutics." Richard S. Jope,* Christopher J. Yuskaitis, and Eléonore Beurel Neurochem Res. 2007; 32(4-5): 577-595.</ref>. | ||
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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).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. | 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,<ref name="SINR"/>. | ||
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. | ||
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== External Ressources == | == External Ressources == | ||
== References == | == References == | ||
{{reflist}} | {{reflist}} | ||