Crystal Structure of the Catalytic Domain of Human Atypical Protein Kinase C-iota Reveals Interaction Mode of Phosphorylation Site in Turn Motif
- 1 September 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 352 (4) , 918-931
- https://doi.org/10.1016/j.jmb.2005.07.060
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Structure of a Cell Polarity Regulator, a Complex between Atypical PKC and Par6 PB1 DomainsJournal of Biological Chemistry, 2005
- The Protein Kinase C Inhibitor Bisindolyl Maleimide 2 Binds with Reversed Orientations to Different Conformations of Protein Kinase APublished by Elsevier ,2004
- Keeping G Proteins at Bay: A Complex Between G Protein-Coupled Receptor Kinase 2 and GßγScience, 2003
- Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigmBiochemical Journal, 2003
- Crystal structure of an activated Akt/Protein Kinase B ternary complex with GSK3-peptide and AMP-PNPNature Structural & Molecular Biology, 2002
- Carboxyl-terminal Phosphorylation Regulates the Function and Subcellular Localization of Protein Kinase C βIIPublished by Elsevier ,1999
- Crystal Structure of the Potent Natural Product Inhibitor Balanol in Complex with the Catalytic Subunit of cAMP-Dependent Protein KinaseBiochemistry, 1999
- Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol esterPublished by Elsevier ,1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformationActa Crystallographica Section D-Biological Crystallography, 1993