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Figure 5.
Figure 5 Structural features at the N and C termini of Ebp1. (A)
The structure shows that the predicted p42 isoform (left) which
starts at Met 55 lacks one and a half helices at the N terminus
of the p48 isoform (indicated in grey in the structure on the
right). This helix makes extensive hydrophobic contacts with the
body of Ebp1 (coloured by atom type: carbon—orange;
nitrogen—blue oxygen—red; sulphur—yellow); its removal
exposes a large hydrophobic cleft on one face of the protein.
The structure of p48 Ebp1 also illustrates the proximity of K20
and K22 to the lys-rich loop 1; together these features may
constitute a bipartite nucleolar localisation signal (Squatrito
et al, 2004; Fujiwara et al, 2006). (B) Position of the
^354LKALL^358 protein-binding motif at the C terminus of Ebp1.
Colouring is the same as in Figure 1B except that residues from
the motifs are highlighted in green. The surface of Ebp1 up to
residue 337 is shown. Close-up views (in similar orientations)
of the LxxLL motif from (C) Ebp1 and (D) the AR ((Hur et al,
2004); PDB—1t7f). Residues from Ebp1 are colour coded as
described above. Carbon atoms of the LxxLL motif of the peptide
ligand of AR are cyan.
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