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Titolo:
Structure of GSK3 beta reveals a primed phosphorylation mechanism
Autore:
ter Haar, E; Coll, JT; Austen, DA; Hsiao, HM; Swenson, L; Jain, J;
Indirizzi:
Vertex Pharmaceut Inc, Cambridge, MA 02139 USA Vertex Pharmaceut Inc Cambridge MA USA 02139 Inc, Cambridge, MA 02139 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 7, volume: 8, anno: 2001,
pagine: 593 - 596
SICI:
1072-8368(200107)8:7<593:SOGBRA>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOGEN-SYNTHASE KINASE-3; BETA-CATENIN; MULTISITE PHOSPHORYLATION; CONSERVED FEATURES; ACTIVATION; INSULIN; FAMILY; CLASSIFICATION; IDENTIFICATION; SPECIFICITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: ter Haar, E Vertex Pharmaceut Inc, 130 Waverly St, Cambridge, MA 02139 USAVertex Pharmaceut Inc 130 Waverly St Cambridge MA USA 02139 SA
Citazione:
E. ter Haar et al., "Structure of GSK3 beta reveals a primed phosphorylation mechanism", NAT ST BIOL, 8(7), 2001, pp. 593-596

Abstract

GSK3 beta was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3 beta prefers prior phosphorylation of its substrates. We present the structureof unphosphorylated GSK3 beta at 2.7 A. The orientation of the two domainsand positioning of the activation loop of GSK3 beta 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 p38 gamma, 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 GSK3 betaand how GSK3 beta relies on a phosphoserine in the substrate for the alignment of the beta- and alpha -helical domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 12:21:41