spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

Right arrow Help viewing high resolution images
Right arrow Return to article
(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.



Fig. 2. Amino acid interactions between the catalytic domain and the autoinhibitory domain regulate UNC-43 calcium-independent activity. (A) Amino acid sequence alignments between rat CaMKI, rat CaMKII and UNC-43 for three key domains: the active site core of the catalytic domain, the C-terminal lobe of the catalytic domain and the autoinhibitory domain. Residues changed in this study are indicated using rat CaMKII numbering. The CaMKII autophosphorylation site, calmodulin (CaM) binding site, and the pseudosubstrate domain are delimited by gray lines below the sequence. The secondary structure elements described for the CaMKI crystal structure are indicated above the lines, using gray boxes for {alpha} helices and white arrows for ß strands (Goldberg et al., 1996). (B) A schematic model for CaMKII and UNC-43 regulatory amino acid interactions between the catalytic domain (the gray box) and the autoinhibitory domain (the black line and gray cylinder). Electrostatic interactions between amino acid side chains are indicated by a dotted line. Hydrophobic pockets created within the catalytic domain are indicated by the white ovals.





Right arrow Return to article