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Figure 1.
Figure 1. Structure of the CASK CaM-Kinase Domain
(A and
B) Ribbon diagrams depicting the overall fold of the CASK
CaM-kinase domain in a complex with 3′-AMP (orthorhombic form,
A; see Figure S3 for the triclinic form) or AMPPNP (triclinic
form, B).
(C and D) Ribbon diagrams of rat CaMKI (C;
Goldberg et al., 1996; PDB ID: 1A06) and rat DAPK1 in a complex
with Mn^2+-AMPPNP (D; Tereshko et al., 2001; PDB ID: 1IG1).
All structures are shown in the same orientation with the
N-terminal lobes (dark gray) at the top and the C-terminal lobes
(light gray) at the bottom. Specific structural elements are
color-coded: portion of the glycine-rich loop (GR-loop) = brown;
catalytic loop (C-loop) = yellow; D/GFG of the Mg^2+ binding
loop = orange (the third residue is disordered in the CaMKI
structure); activation segment = green; C-terminal
Ca^2+/CaM-binding segment (CaM-segment) = red. Bound nucleotides
in (A) (3′-AMP), (B) (5′-AMP portion of AMPPNP), and (D)
(AMPPNP) are shown in ball-and-sticks.
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