2F86

The Association Domain of C. elegans CaMKII

2F86 の概要

• エントリーDOI: 10.2210/pdb2f86/pdb
• 分子名称: Hypothetical protein K11E8.1d (2 entities in total)
• 機能のキーワード: unc-43; oligomerization domain, transferase
• 由来する生物種: Caenorhabditis elegans
• 細胞内の位置: Cytoplasm : O62305
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 115236.28

構造登録者

Rosenberg, O.S.,Kuriyan, J. (登録日: 2005-12-01, 公開日: 2006-02-07, 最終更新日: 2023-08-30)

主引用文献

Rosenberg, O.S.,Deindl, S.,Comolli, L.R.,Hoelz, A.,Downing, K.H.,Nairn, A.C.,Kuriyan, J.
Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II.
Febs J., 273:682-694, 2006

PubMed Abstract: 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.

PubMed: 16441656
DOI: 10.1111/j.1742-4658.2005.05088.x

実験手法

X-RAY DIFFRACTION (2.64 Å)