Sandbox Reserved 433
From Proteopedia
(Difference between revisions)
| Line 13: | Line 13: | ||
==Overall Structure== | ==Overall Structure== | ||
| + | -Monomeric | ||
| + | |||
-Glycogen Synthase Kinase-3 (GSK-3) is a serine/threonine protein kinase | -Glycogen Synthase Kinase-3 (GSK-3) is a serine/threonine protein kinase | ||
| + | |||
-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. | ||
| + | |||
-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) | ||
| + | |||
-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 | ||
| - | -Classified the PDB structures into three groups | + | |
| + | -Classified the PDB structures into three groups | ||
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 22:09, 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. |
| |||||||||||
