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Figure 1.
Figure 1. Uninhibited HGFA. Schematic representation of the
crystallized HGFA 34 kDa fragment (starting at residue 373),
looking into the substrate binding/active site region. Disulfide
links are labeled. Cys168 was modeled with two side-chain
conformations, only one of which makes a bond to Cys182. Cys187
is unpaired. An eight-residue section of the HGFA light chain
(green) can be seen in the rear, including its disulfide link to
the protease domain (Cys394/Cys122). Loops colored pink differ
structurally among homologous enzymes and help determine
inhibitor and substrate specificity. The crystallized construct
in the context of intact HGFA is depicted at the bottom.
Molecular images produced using PyMOL (Delano Scientific, San
Carlos CA).
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