The structural basis for substrate recognition and control by protein kinases1
Open Access
- 23 June 1998
- journal article
- lecture
- Published by Wiley in FEBS Letters
- Vol. 430 (1-2) , 1-11
- https://doi.org/10.1016/s0014-5793(98)00606-1
Abstract
Protein kinases catalyse phospho transfer reactions from ATP to serine, threonine or tyrosine residues in target substrates and provide key mechanisms for control of cellular signalling processes. Th...Keywords
This publication has 48 references indexed in Scilit:
- The 2.35 å crystal structure of the inactivated form of chicken src: a dynamic molecule with multiple regulatory interactionsJournal of Molecular Biology, 1997
- Kinase conformations: A computational study of the effect of ligand bindingProtein Science, 1997
- Activation Mechanism of the MAP Kinase ERK2 by Dual PhosphorylationCell, 1997
- A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibilityStructure, 1997
- Crystal structure of the Src family tyrosine kinase HckNature, 1997
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- Three-dimensional Structure of Mammalian Casein Kinase I: Molecular Basis for Phosphate RecognitionJournal of Molecular Biology, 1996
- Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and productStructure, 1995
- Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptideBiochemistry, 1993
- Structural mechanism for glycogen phosphorylase control by phosphorylation and AMPJournal of Molecular Biology, 1991