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. 2010 Nov 19;286(3):2022–2030. doi: 10.1074/jbc.M110.197178

FIGURE 4.

FIGURE 4.

Conservation of AP-1 and AP-3 residues potentially involved in interactions with (D/E)XXXL(L/I) signals. A, alignment of human σ1A (RefSeq accession no. NP_001274), σ2 (GenBankTM accession no. AAH06337), and σ3A (GenBankTM accession no. CAG29337). The alignment shows the conservation of σ2 residues (Arg15, Ala63, Val88, Asn92, Glu100, Leu101, and Leu103 shown in black boxes) that interact with residues at different positions of the CD4 Q-peptide (20). Shown in black lettering are the positions on the signal (residue at −4; LL, dileucine pair; or O, other) proposed to bind to the σ residues in the corresponding boxes. B, alignment of N-terminal sequences of human γ1 (GenBankTM accession no. AAH36283), αC (Swiss-Prot accession no. O94973) and δ (GenBankTM accession number AAC51761) showing the conservation of the α subunit Arg residue (αArg15, shown in the black box) proposed to stabilize the −4 position of the CD4 Q-peptide (20). Alignments were generated with CLC Sequence Viewer; decreasing conservation of residues is shown by red to blue rainbow coloring.