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Figure 2.
Figure 2 (A) Side view of the SNX9 PX-BAR dimer structure ribbon
diagram. BAR domains are shown in red, PX in blue, and the novel
Yoke (Y) subdomain in yellow. N- and C-termini are labeled. (B)
Top view of the SNX9 PX-BAR dimer structure. The domains are
labeled. (C) Ribbon representation of SNX9 Yoke (Y) subdomain
structure. The Yoke domain consists of two parts: Y[N] derived
from amino-acid residues 214–250 and Y[C] from 375–390.
Secondary structure elements are labeled. (D) Sequence alignment
of human SNX9 (Q9Y5X1), SNX18 (AAH67860), and SNX30 (ABN09670)
PX-BAR domains. The proteins represent a subfamily of PX-BAR
SNXs. Secondary structure elements corresponding to the SNX9
structure are monitored. Coloring corresponds to that from
panels A–C. Helices are labeled with H,  -strands
with S, and P denotes a proline-rich motif. The amino-acid
residues involved in the dimerization are labeled (+,
hydrophobic bar–bar contacts; ^*, H-bond bar–bar contacts),
as well as residues involved in interdomain interaction (§,
hydrophobic bar-px:y contacts; &, H-bonds bar-px:y contacts).
Symbols of consensus sequence are: 2, E/Q; 3, T/S; 4, K/R; 5,
Y/F; and 6, hydrophobic.
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