1l7z: Difference between revisions
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'''Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide''' | {{Structure | ||
|PDB= 1l7z |SIZE=350|CAPTION= <scene name='initialview01'>1l7z</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L7Z is a [ | 1L7Z is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7Z OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14765114 14765114] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:40 2008'' |
Revision as of 13:27, 20 March 2008
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, resolution 2.3Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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. 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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