1l7z
From Proteopedia
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==Overview== | ==Overview== | ||
| - | A variety of viral and signal transduction proteins are known to be | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Matsubara, M.]] | [[Category: Matsubara, M.]] | ||
[[Category: Nakatsu, T.]] | [[Category: Nakatsu, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Taniguchi, H.]] | [[Category: Taniguchi, H.]] | ||
[[Category: Yamauchi, E.]] | [[Category: Yamauchi, E.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:22 2008'' |
Revision as of 11:42, 21 February 2008
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Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide
Contents |
Overview
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.
Disease
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 Structure
1L7Z is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:42:22 2008
Categories: Homo sapiens | Protein complex | Kato, H. | Matsubara, M. | Nakatsu, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Taniguchi, H. | Yamauchi, E. | CA | MYR | Calmodulin | Myristoylation | Protein-protein interaction | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
