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The overall structure of the Glycogen Synthase Kinase-3β (GSK-β) enzyme is a monomer, and is similar to that of the apoenzyme. GSK-3β has a two-domain kinase fold with a β-strand domain (shown in light blue) at the N-terminus, and an α-helical domain (shown in red) at the C-terminus. Bordering the ATP-binding site is a hinge and glycine-rich loop, found at the boundary of the α-helical and β-strand domain. The activation loop, found along the surface of the substrate-binding groove, can be seen in the (shown in green). The C-terminal resides form a domain that packs against the α -helical domain, which are outside the main kinase fold. The β-strand domain consists of seven β-strands that run in an antiparallel formation. These seven strands include a β -barrel that is interrupted in the middle by a short helix (shown in orange) that packs against the β-barrel. Two of the helixes residues, which are conserved in all kinases, play key roles in the catalytic action of the enzyme. Ser9 is one phosphorylation site that is responsible for the inactivation of GSK-3 β, and the phosphorylation of site Tyr210 is responsible for increasing the catalytic activity. Tyr201 is found on the activation loop, in (green). | The overall structure of the Glycogen Synthase Kinase-3β (GSK-β) enzyme is a monomer, and is similar to that of the apoenzyme. GSK-3β has a two-domain kinase fold with a β-strand domain (shown in light blue) at the N-terminus, and an α-helical domain (shown in red) at the C-terminus. Bordering the ATP-binding site is a hinge and glycine-rich loop, found at the boundary of the α-helical and β-strand domain. The activation loop, found along the surface of the substrate-binding groove, can be seen in the (shown in green). The C-terminal resides form a domain that packs against the α -helical domain, which are outside the main kinase fold. The β-strand domain consists of seven β-strands that run in an antiparallel formation. These seven strands include a β -barrel that is interrupted in the middle by a short helix (shown in orange) that packs against the β-barrel. Two of the helixes residues, which are conserved in all kinases, play key roles in the catalytic action of the enzyme. Ser9 is one phosphorylation site that is responsible for the inactivation of GSK-3 β, and the phosphorylation of site Tyr210 is responsible for increasing the catalytic activity. Tyr201 is found on the activation loop, in (green). | ||
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| - | Haar, Ernst ter., Coll, Joyce T., Austen, Douglas A., Hsiao, Hsun-Mei., Swenson, Lora., Jain, Jugnu. Structure of GSK3B reveals a primed phosphorylation mechanism. Vertex Pharmaceuticals Incoprporated, Cambridge MA. Nature Publishing Group, Vol 8 No 7. July 2001. | ||
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*[http://www.proteopedia.org/wiki/index.php/3pup Glycogen Synthase Kinase 3 beta (GSK3B) complexed with a ruthenium octasporine ligand (OS1)] | *[http://www.proteopedia.org/wiki/index.php/3pup Glycogen Synthase Kinase 3 beta (GSK3B) complexed with a ruthenium octasporine ligand (OS1)] | ||
| + | Works Cited | ||
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| + | Haar, Ernst ter., Coll, Joyce T., Austen, Douglas A., Hsiao, Hsun-Mei., Swenson, Lora., Jain, Jugnu. Structure of GSK3B reveals a primed phosphorylation mechanism. Vertex Pharmaceuticals Incoprporated, Cambridge MA. Nature Publishing Group, Vol 8 No 7. July 2001. | ||
==Credits== | ==Credits== | ||
Revision as of 18:41, 2 April 2015
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