1IWQ

Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin

Summary for 1IWQ

• Entry DOI: 10.2210/pdb1iwq/pdb
• Descriptor: CALMODULIN, MARCKS, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: calmodulin-target peptide complex, riken structural genomics/proteomics initiative, rsgi, structural genomics, metal binding protein-protein binding complex, metal binding protein/protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton, spindle: P62158; Cytoplasm, cytoskeleton (Probable): P26645
• Total number of polymer chains: 2
• Total formula weight: 19215.52

Authors

Yamauchi, E.,Nakatsu, T.,Matsubara, M.,Kato, H.,Taniguchi, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-05-31, release date: 2003-03-11, Last modification date: 2023-10-25)

Primary citation

Yamauchi, E.,Nakatsu, T.,Matsubara, M.,Kato, H.,Taniguchi, H.
Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca(2+)-calmodulin
NAT.STRUCT.BIOL., 10:226-231, 2003

PubMed 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.

PubMed: 12577052
DOI: 10.1038/nsb900

Experimental method

X-RAY DIFFRACTION (2 Å)