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==Overall Structure== | ==Overall Structure== | ||
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-Glycogen Synthase Kinase-3 (GSK-3) is a serine/threonine protein kinase | -Glycogen Synthase Kinase-3 (GSK-3) is a serine/threonine protein kinase | ||
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-2 isoforms: alpha and beta, that are 97% homologous in their catalytic domain, but diverse at the N and C terminus. | -2 isoforms: alpha and beta, that are 97% homologous in their catalytic domain, but diverse at the N and C terminus. | ||
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-Both isoforms have a conserved N-terminal serine reside (S21 for alpha and S9 for beta) | -Both isoforms have a conserved N-terminal serine reside (S21 for alpha and S9 for beta) | ||
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-Phosphorylation of the N-terminal serine residue plays an important role for further activity | -Phosphorylation of the N-terminal serine residue plays an important role for further activity | ||
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Mishra, Nibha et al. Structure based virtual screening of GSK-3beta: Importance of protein flexibility and induced fit, 2009. Bioorganic & Medicinal Chemistry Letters, 2009, Vol. 19 Iss. 19, pp. 5582-5585. Retreived from http://www.sciencedirect.com/science/article/pii/S0960894X09011780 | Mishra, Nibha et al. Structure based virtual screening of GSK-3beta: Importance of protein flexibility and induced fit, 2009. Bioorganic & Medicinal Chemistry Letters, 2009, Vol. 19 Iss. 19, pp. 5582-5585. Retreived from http://www.sciencedirect.com/science/article/pii/S0960894X09011780 | ||
Revision as of 22:12, 12 March 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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