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Figure 1.
Figure 1. Identification and solution NMR structure of PB2
C-terminal domain. (a) Protein expression screen of 26,880
random deletion constructs of the pb2 gene. Stable expression of
soluble protein results in efficient in vivo labeling of a
C-terminal biotin acceptor peptide. Detection is by fluorescent
streptavidin and fluorimaging. (b) Ribbon diagram of the ten
lowest-energy NMR structures superimposed using backbone heavy
atoms (r.m.s. deviation 0.94 Å for 224 atoms). Indicated
are Asp701, Arg702 and Ser714, which are implicated in
cross-species transmission, and basic regions corresponding to
the minor (purple) and major (gold) sites of the bipartite NLS.
(c) Primary sequence alignment comparing influenza (FLU) A, B
and C strains. Indicated are residues implicated in
cross-species transmission (blue triangles), the minor site
(purple triangles) and major site (gold triangles) of the
bipartite NLS, conserved buried hydrophobic residues (black
ovals) and secondary structure elements.
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