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Figure 2.
Figure 2. A representation of ATF binding to uPAR. Domains
D^I (amino acid residues 1–93), D^II (residues 94–191) and
D^III (residues 192–277) of suPAR are shown in yellow, blue,
and red, respectively; KD (residues 47–132) is in green, GFD
(residues 10–46) in magenta. (a) A cartoon representation of
the suPAR[2345]/ATF complex. The individual β-strands of
suPAR[2345] are labeled according to Llinas et al.^30 and Low et
al.^31 Domain D^I: βIA (residues 2–8), βIB (13–17), βIC
(24–33), βID (38–45), βIE (53–59), and βIF (63–70);
domain D^II: βIIA (94–100), βIIB (112–115), βIIC
(122–129), βIID (143–149), βIIE (156–161), and βIIF
(163–171); domain D^III: βIIIA (195–199), βIIIB
(211–214), βIIIC (222–229), βIIID (236–243), and βIIIE
(259–267). Contacts between the domains are mediated
via interactions βIE and βIID (domains D^I and D^II), βIIE
and βIIID (domains D^II and D^III). (b) The ATF (cartoon
representation) binds to the central cavity of suPAR[2345]
(surface representation) and the Ω-loop (Cys19–Cys31,
ball-and-sticks) is primarily responsible for the high-affinity
binding. Residues of suPAR[2345] interacting with ATF are in
cyan.
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