1l7z
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Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this StructureAbout this Structure
1L7Z is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin., Matsubara M, Nakatsu T, Kato H, Taniguchi H, EMBO J. 2004 Feb 25;23(4):712-8. Epub 2004 Feb 12. PMID:14765114
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