Details

Autor(en) / Beteiligte

• Rao, Vibha D
• Misra, Saurav
• Boronenkov, Igor V
• Anderson, Richard A
• Hurley, James H

Titel

Structure of Type IIβ Phosphatidylinositol Phosphate Kinase: A Protein Kinase Fold Flattened for Interfacial Phosphorylation

Ist Teil von

• Cell, 1998-09, Vol.94 (6), p.829-839

Ort / Verlag

Elsevier Inc

Erscheinungsjahr

1998

Link zum Volltext

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• Phosphoinositide kinases play central roles in signal transduction by phosphorylating the inositol ring at specific positions. The structure of one such enzyme, type IIβ phosphatidylinositol phosphate kinase, reveals a protein kinase ATP-binding core and demonstrates that all phosphoinositide kinases belong to one superfamily. The enzyme is a disc-shaped homodimer with a 33 × 48 Å basic flat face that suggests an electrostatic mechanism for plasma membrane targeting. Conserved basic residues form a putative phosphatidylinositol phosphate specificity site. The substrate-binding site is open on one side, consistent with dual specificity for phosphatidylinositol 3- and 5-phosphates. A modeled complex with membrane-bound substrate and ATP shows how a phosphoinositide kinase can phosphorylate its substrate in situ at the membrane interface.