2f86
From Proteopedia
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| - | [[Image:2f86.gif|left|200px]] | + | [[Image:2f86.gif|left|200px]] |
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| - | '''The Association Domain of C. elegans CaMKII''' | + | {{Structure |
| + | |PDB= 2f86 |SIZE=350|CAPTION= <scene name='initialview01'>2f86</scene>, resolution 2.64Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''The Association Domain of C. elegans CaMKII''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F86 is a [ | + | 2F86 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F86 OCA]. |
==Reference== | ==Reference== | ||
| - | Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:[http:// | + | Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16441656 16441656] |
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: unc-43; oligomerization domain]] | [[Category: unc-43; oligomerization domain]] | ||
| - | ''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 16:49:14 2008'' |
Revision as of 14:49, 20 March 2008
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| , resolution 2.64Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Association Domain of C. elegans CaMKII
Overview
Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C-terminal region of approximately 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6-fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIalpha has revealed a tetradecameric assembly with two stacked 7-fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6-fold symmetric state by the interactions of the N-terminal approximately 1-335 residues and that the removal of this region allows the association domain to convert into a more stable 7-fold symmetric form.
About this Structure
2F86 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:16441656
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