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Figure 5.
FIGURE 5. Comparative views of the active sites of hMIF and
AceMIF. A, view into the cavity of the active sites of AceMIF
and hMIF. The figure shows the substrate HPP bound in the active
site of hMIF (50), which is displayed in stick representation.
B, superposition of the active sites of AceMIF and hMIF, with
HPP bound to hMIF. Residues within hydrogen-bonding distance to
HPP are colored in red (AceMIF) or yellow (hMIF). Residue codes
correspond to AceMIF. Residues in parentheses correspond to
hMIF. Two adjacent protomers (colored in cyan and green) in the
trimer form the active site, and there are three active sites in
each trimer. C, hydrogen bonds and hydrophobic interactions
between HPP and interacting residues in a model of AceMIF:HPP
and the crystal structure of hMIF:HPP (50), respectively, are
shown. The residues involved in hydrophobic interactions with
HPP are drawn as a spiked hemisphere. Distances for hydrogen
bonds are in green dashed lines with their distance in Angstrom
units.
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