2f86 | pdb_00002f86

The Association Domain of C. elegans CaMKII

spinqualitylabelsall models 2f86, resolution 2.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f86 is a 7 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.64Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCC2D_CAEEL Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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