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Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin
- Source :
- Nature Structural and Molecular Biology; March 2003, Vol. 10 Issue: 3 p226-231, 6p
- Publication Year :
- 2003
-
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 Šresolution 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.
Details
- Language :
- English
- ISSN :
- 15459993 and 15459985
- Volume :
- 10
- Issue :
- 3
- Database :
- Supplemental Index
- Journal :
- Nature Structural and Molecular Biology
- Publication Type :
- Periodical
- Accession number :
- ejs25308054
- Full Text :
- https://doi.org/10.1038/nsb900