Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin
- 10 February 2003
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 10 (3) , 226-231
- https://doi.org/10.1038/nsb900
Abstract
The calmodulin-binding domain of myristoylated alanine-rich C kinase substrate (MARCKS), which interacts with various targets including calmodulin, actin and membrane lipids, has been suggested to function as a crosstalk point among several signal transduction pathways. We present here the crystal structure at 2 Å resolution of a peptide consisting of the MARCKS calmodulin (CaM)-binding domain in complex with Ca2+-CaM. The domain assumes a flexible conformation, and the hydrophobic pocket of the calmodulin N-lobe, which is a common CaM-binding site observed in previously resolved Ca2+-CaM–target peptide complexes, is not involved in the interaction. The present structure presents a novel target-recognition mode of calmodulin and provides insight into the structural basis of the flexible interaction module of MARCKS.Keywords
This publication has 39 references indexed in Scilit:
- Tob-Mediated Cross-Talk between MARCKS Phosphorylation and ErbB-2 ActivationBiochemical and Biophysical Research Communications, 2001
- The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-BisphosphateJournal of Biological Chemistry, 2001
- Rho-Associated Kinase Phosphorylates MARCKS in Human Neuronal CellsBiochemical and Biophysical Research Communications, 2001
- A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studiesJournal of Molecular Biology, 2000
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+ Pump,Biochemistry, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163FEBS Letters, 1996
- Defining Protein−Protein Interactions Using Site-Directed Spin-Labeling: The Binding of Protein Kinase C Substrates to CalmodulinBiochemistry, 1996
- MARCKS deficiency in mice leads to abnormal brain development and perinatal death.Proceedings of the National Academy of Sciences, 1995