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Figure 5.
Figure 5. Repositioning of the “integrin-interacting”
loop (Trp129–Arg142) in suPAR[2345] upon ATF binding.
Interactions between amino acid residues Cys19–Lys23 of the
ATF and Pro138–Asp140 of suPAR[2345] leads to bending of the
loop towards the central cavity of the receptor. (a) The
complexes, suPAR[2345]/ATF (domains D^I, D^II and D^III colored
yellow, blue and red, respectively) and suPAR/AE147 (shown in
gray), were aligned on the basis of the corresponding C^α atoms
of domain D^I only. GFD is shown as a combination of
ball-and-sticks and semi-transparent surface. The βIIC-βIID
hairpin is in cartoon representation and its residues
interacting with GFD as ball-and-sticks. (b) A detailed view of
residues engaged in the interactions between strands βIIC and
βIID of suPAR[2345] and the Ω-loop of ATF. The Ω-loop is
shown in surface representation and the interacting residues
contributed by domain D^II are shown as balls-and-sticks. Note
the major movement of the βIIC-βIID hairpin caused by
interactions with the Ω-loop. In both structures, amino acid
residues 132 through 136 of suPAR are missing.
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