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1l7z
From Proteopedia
(New page: 200px<br /> <applet load="1l7z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l7z, resolution 2.3Å" /> '''Crystal structure of...) |
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caption="1l7z, resolution 2.3Å" /> | caption="1l7z, resolution 2.3Å" /> | ||
'''Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide'''<br /> | '''Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L7Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1L7Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:16:48 2008'' |
Revision as of 14:16, 15 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 Fri Feb 15 16:16:48 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
