1L7Z

Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide

Summary for 1L7Z

• Entry DOI: 10.2210/pdb1l7z/pdb
• Descriptor: CALMODULIN, CAP-23/NAP-22, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: calmodulin, myristoylation, protein-protein interaction, 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
• Total number of polymer chains: 2
• Total formula weight: 18088.29

Authors

Matsubara, M.,Nakatsu, T.,Yamauchi, E.,Kato, H.,Taniguchi, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-03-18, release date: 2003-09-16, Last modification date: 2024-11-06)

Primary citation

Matsubara, M.,Nakatsu, T.,Kato, H.,Taniguchi, H.
Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin
EMBO J., 23:712-718, 2004

PubMed Abstract: A variety of viral and signal transduction proteins are known to be myristoylated. Although the role of myristoylation in protein-lipid interaction is well established, the involvement of myristoylation in protein-protein interactions is less well understood. CAP-23/NAP-22 is a brain-specific protein kinase C substrate protein that is involved in axon regeneration. Although the protein lacks any canonical calmodulin (CaM)-binding domain, it binds CaM with high affinity. The binding of CAP-23/NAP-22 to CaM is myristoylation dependent and the N-terminal myristoyl group is directly involved in the protein-protein interaction. Here we show the crystal structure of Ca2+-CaM bound to a myristoylated peptide corresponding to the N-terminal domain of CAP-23/NAP-22. The myristoyl moiety of the peptide goes through a hydrophobic tunnel created by the hydrophobic pockets in the N- and C-terminal domains of CaM. In addition to the myristoyl group, several amino-acid residues in the peptide are important for CaM binding. This is a novel mode of binding and is very different from the mechanism of binding in other CaM-target complexes.

PubMed: 14765114
DOI: 10.1038/sj.emboj.7600093

Experimental method

X-RAY DIFFRACTION (2.3 Å)