JCS02995 Supplementary Material

Files in this Data Supplement:

• Supplemental Figure 1 -

  Fig. S1. p75 residues Lys360 (K360), Ile365 (I365), Val370 (V370) and Phe406 (F406) contribute to recognition of JPO2. (A) HA-p75 (wt) or the indicated point mutant was co-expressed with FLAG-JPO2 in 293T cells, and lysates were immunoprecipitated with anti-Flag affinity beads. Input and immunoprecipitated proteins were detected by western blotting. (B) Ribbon diagram of the p75 IBD (Cherepanov et al., 2005a) (PDB accession 2B4J, chain C). Side chains of residues Lys360, Ile365, Val370 and Phe406, implicated in the interaction with JPO2, are shown as sticks. Whereas residues Lys360 and Val370 (purple) are involved in JPO2 binding, residues Ile365 and Phe406 (pink) participate in binding to JPO2 and HIV-1 IN. Asp366 (blue), essential for the interaction with HIV-1 IN (Cherepanov et al., 2005b), does not readily contribute to the interaction with JPO2 (see A). The figure was created using MolMol (Koradi et al., 1996).

• Supplemental Figure 2 -

  Fig. S2. Sequence alignment of human JPO1, JPO2 and amphibian JPOL. Known functional and predicted structural elements of JPO2 are indicated. Residue numbering corresponds to the human sequence. Sequence identity across the homologs is indicated in red, and sequence identity in at least 70% of the homologs and conservative mutations are in yellow. The minimal p75-binding region (residues 58-119) is indicated by a solid line; the dotted line extends to residue 128 (Fig. 5). The alignment was created using ESPript (Gouet et al., 1999).