Sandbox28
From Proteopedia
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Glycogen Synthase Kinase 3 Beta has <scene name='Sandbox28/Beta_sheets/1'>beta sheet</scene> | Glycogen Synthase Kinase 3 Beta has <scene name='Sandbox28/Beta_sheets/1'>beta sheet</scene> | ||
in the two opposite quadrants and <scene name='Sandbox28/Alpha_helix/1'>alpha helices</scene> in the other two opposite quadrants. | in the two opposite quadrants and <scene name='Sandbox28/Alpha_helix/1'>alpha helices</scene> in the other two opposite quadrants. | ||
| - | There are also two active sites that can be seen here: <scene name='Sandbox28/ | + | There are also two active sites that can be seen here: <scene name='Sandbox28/Active_sites/1'>Active Sites</scene> |
| - | + | ||
This view shows a | This view shows a | ||
<scene name='Sandbox28/Hydrophobicalpha/1'>hydrophobic element</scene> of an alpha helix (in red) on the surface of the protein. | <scene name='Sandbox28/Hydrophobicalpha/1'>hydrophobic element</scene> of an alpha helix (in red) on the surface of the protein. | ||
Revision as of 16:45, 4 March 2009
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
Bejan Hakimi and Brendan Walker 3/4/09
GLYCOGEN SYNTHASE KINASE 3 BETA
Glycogen Synthase Kinase 3 Beta has in the two opposite quadrants and in the other two opposite quadrants. There are also two active sites that can be seen here: This view shows a of an alpha helix (in red) on the surface of the protein.
Publication Abstract from PubMed
Glycogen synthase kinase 3 beta (GSK3 beta) plays a key role in insulin and Wnt signaling, phosphorylating downstream targets by default, and becoming inhibited following the extracellular signaling event. The crystal structure of human GSK3 beta shows a catalytically active conformation in the absence of activation-segment phosphorylation, with the sulphonate of a buffer molecule bridging the activation-segment and N-terminal domain in the same way as the phosphate group of the activation-segment phospho-Ser/Thr in other kinases. The location of this oxyanion binding site in the substrate binding cleft indicates direct coupling of P+4 phosphate-primed substrate binding and catalytic activation, explains the ability of GSK3 beta to processively hyperphosphorylate substrates with Ser/Thr pentad-repeats, and suggests a mechanism for autoinhibition in which the phosphorylated N terminus binds as a competitive pseudosubstrate with phospho-Ser 9 occupying the P+4 site.
Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition., Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH, Cell. 2001 Jun 15;105(6):721-32. PMID:11440715
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
