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PMID:12577052
| Citation |
Yamauchi, E, Nakatsu, T, Matsubara, M, Kato, H and Taniguchi, H (2003) Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat. Struct. Biol. 10:226-31 |
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| 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 A 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. |
| Links |
PubMed Online version:10.1038/nsb900 |
| Keywords |
Amino Acid Sequence; Binding Sites; Calcium/chemistry; Calmodulin/chemistry; Calmodulin/metabolism; Crystallography, X-Ray; Hydrophobic and Hydrophilic Interactions; Intracellular Signaling Peptides and Proteins; Macromolecular Substances; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Peptides/chemistry; Peptides/metabolism; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Protein Conformation; Protein Structure, Tertiary |
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