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Figure 5.
Figure 5. The HGFA/KD1 complex. (a) The conventional
conformation of the HGFA substrate binding region from the
HAI-1-KD1 complex (light brown) compared to the unconventional
conformation from uninhibited HGFA (blue). (b) Overall view with
HGFA surface (light brown/red) and KD1 (green/yellow), including
side-chains form Arg13(258), Arg15(260), and Phe18(263). The
(N-terminal affinity tag + KD1) construct in the context of
HAI-1B is depicted at the bottom. Prominent residues from the
HGFA 37-loop, 60-loop and 99-loop are labeled. Red and yellow
colors are residues of HGFA (red) and KD1 (yellow) with an atom
within 3.5 Å of the other protein. (c) Details of the
interaction between HGFA and HAI-1-KD1, in the same orientation
as above. Portions of the KD1 domain (yellow) are depicted in
the HGFA (light brown) active site. H-bonds between KD1 and HGFA
are grey/black dotted lines. Inhibitor residue labels are
underlined.
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