Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin

Nat Struct Biol. 2003 Mar;10(3):226-31. doi: 10.1038/nsb900.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Peptides / chemistry
  • Peptides / metabolism
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism*
  • Protein Conformation
  • Protein Structure, Tertiary


  • Calmodulin
  • Intracellular Signaling Peptides and Proteins
  • Macromolecular Substances
  • Membrane Proteins
  • Peptides
  • Phosphoproteins
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Calcium

Associated data

  • PDB/1IWQ