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Figure 1.
Fig. 1. Structure of the TnC/TnI[1-47] complex. (A)
Ribbon diagram of the TnC/TnI[1-47] complex structure. The  -helices,
 -strands,
and loops of TnC are in red, green, and yellow, respectively.
The unwound and kinked central D/E -helix of
TnC is shown in blue, and the interdomain extended linker is
black. The two calcium ions in the TnC C-lobe are shown as black
balls. The TnI[1-47] -helix is
in cyan. The figure was drawn with the MOLSCRIPT program (21).
(B) Hydrophobic (green arrows) and polar (red arrows) side-chain
interactions between TnI[1-47] (circles) and TnC (rectangles)
residues in the TnC/TnI[1-47] complex. The hydrophobic and polar
residues are shown in green and red, respectively. Water
molecules are shown as cyan hexagons. Main chain carbonyl
oxygens of the interacting amino acids are shown as a red O
attached to the subsequent residues. (C) Portion of the final
(2Fo-Fc) electron density map and the TnC/TnI[1-47] model (ball
and stick) in the hydrophobic cavity of the C-lobe of TnC. The
TnI and TnC residues are shown in cyan and atom-dependent (C, N,
O, and S are yellow, blue, red, and green, respectively) colors,
respectively. Met-21, protruding into hydrophobic cleft of TnC,
is colored red. The figure was produced with the O program (19).
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