Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin.
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.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Calcium, Calmodulin, Crystallography, X-Ray, Hydrophobicity, Intracellular Signaling Peptides and Proteins, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Peptides, Phosphoproteins, Protein Conformation, Protein Structure, Tertiary
Amino Acid Sequence, Binding Sites, Calcium, Calmodulin, Crystallography, X-Ray, Hydrophobicity, Intracellular Signaling Peptides and Proteins, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Peptides, Phosphoproteins, Protein Conformation, Protein Structure, Tertiary
Nat. Struct. Biol.
Date: Mar. 01, 2003
PubMed ID: 12577052
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