1I09

STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)

1I09 の概要

• エントリーDOI: 10.2210/pdb1i09/pdb
• 分子名称: GLYCOGEN SYNTHASE KINASE-3 BETA, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: kinase, beta barrel, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P49841
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93982.31

構造登録者

Ter Haar, E.,Coll, J.T.,Jain, J. (登録日: 2001-01-29, 公開日: 2002-01-01, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)