Figure 3 - full size

 

Figure 3.
Figure 3. Structure of KChIP1*-Kv4.2N30(A) Stereo cylinder view of KChIP1* monomer showing the coordination of four EF-hands (helix 2 to 5, N lobe, in cyan; helix 6 to 9, C lobe, in blue) and the central groove bound by H10 (yellow) and α1 (red) helices. α1 is bent at Pro10. The N-terminal helix (H1) is shown in yellow.(B) Stereo view of the KChIP1*-Kv4.2N30 dimeric complex, which is 90° rotated around the horizontal axis from view A. The 2-fold axis lies at the center of the dimer and perpendicular to the paper. The molecules are colored in the same way as (A). The residues 21–30 of Kv4.2N30 lacking electron density are not shown. Dots represent residues 160–170 of KChIP1* that lack electron density. Calcium ions (spheres) are bound to EF-3 and EF-4.(C) Comparison of the loops from four EF-hands of KChIP1*. Canonical Ca^2+-coordinating positions are numbered (Figure 1A). Five out of seven Ca^2+-coordinating oxygens (red) are from side chains of four conserved residues (position 1, 3, 5, 12) and one from a backbone carboxy-group (position 7). Calcium-loaded EF-3 and EF-4 have an extra oxygen from water molecule. Position 1 of EF-1 is not shown because it is part of helix (E1). Blue atoms are nitrogens.

The above figure is reprinted by permission from Cell Press: Neuron (2004, 41, 573-586) copyright 2004.