1I09

STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)

Summary for 1I09

• Entry DOI: 10.2210/pdb1i09/pdb
• Descriptor: GLYCOGEN SYNTHASE KINASE-3 BETA, PHOSPHATE ION (3 entities in total)
• Functional Keywords: kinase, beta barrel, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P49841
• Total number of polymer chains: 2
• Total formula weight: 93982.31

Authors

Ter Haar, E.,Coll, J.T.,Jain, J. (deposition date: 2001-01-29, release date: 2002-01-01, Last modification date: 2024-02-07)

Primary citation

ter Haar, E.,Coll, J.T.,Austen, D.A.,Hsiao, H.M.,Swenson, L.,Jain, J.
Structure of GSK3beta reveals a primed phosphorylation mechanism.
Nat.Struct.Biol., 8:593-596, 2001

PubMed Abstract: GSK3beta was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3beta prefers prior phosphorylation of its substrates. We present the structure of unphosphorylated GSK3beta at 2.7 A. The orientation of the two domains and positioning of the activation loop of GSK3beta are similar to those observed in activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of the phosphothreonine in activated p38gamma, CDK2 or ERK2. A loop from a neighboring molecule in the crystal occupies a portion of the substrate binding groove. The structure explains the unique primed phosphorylation mechanism of GSK3beta and how GSK3beta relies on a phosphoserine in the substrate for the alignment of the beta- and alpha-helical domains.

PubMed: 11427888
DOI: 10.1038/89624

Experimental method

X-RAY DIFFRACTION (2.7 Å)