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==Overall Structure== | ==Overall Structure== | ||
| - | -GSK- | + | 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 (blue, residues 25-138) at the N-terminus, and an α-helical domain (red, residues 139-343) 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 (green, residues 200-226). 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 (orange, residue 96-102) 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 ATP-binding site is at the interface of the alpha-helical and beta-strand domain and is bordered by the glycine-rich loop and the hinge | ||
| - | -The activation loop runs along the surface of the substrate binding groove | ||
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| - | -The C-terminal residues are outside the core kinase fold and form a small domain that packs against the alpha-helical domain | ||
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| - | -The beta-strand domain consists of seven antiparallel beta-strands | ||
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| - | -Two phosphorylation sites that influence the catalytic activity of the protein | ||
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. | 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. | ||
| - | -Monomer | ||
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| - | -Overall structures of the enzyme are similar to that of the apoenzyme | ||
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| - | -The crystals contain two molecules of GSK-3beta in the asymmetric unit and the two molecules are treated as identical | ||
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| - | -Glycogen Synthase Kinase-3 (GSK-3) is a serine/threonine protein kinase | ||
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| - | -Both isoforms have a conserved N-terminal serine reside (S21 for alpha and S9 for beta) | ||
| - | -Phosphorylation of the N-terminal serine residue plays an important role for further activity | ||
Revision as of 18:13, 2 April 2015
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
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