|
Figure 4.
The dimer interface for the influenza A/Udorn/72 NS1A
effector domain. (a) A space-filling model of monomer subunit A
reveals a distinct largely hydrophobic pocket that has evolved
to bind aromatic residues from the F2F3 domain of CPSF30. Here,
Trp187 from effector domain monomer subunit B (shown in blue)
binds in that pocket. (b) A detailed view of the interactions of
Trp187 with monomer subunit A binding-cleft residues (shown in
green). Acta Crystallogr D Biol Crystallogr. 2009 January 1;
65(Pt 1): 11–17. Published online 2008 December 19. doi:
10.1107/S0907444908032186. Copyright [copyright] International
Union of Crystallography 2009
|
