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Fig. 1 | Retrovirology

Fig. 1

From: Role of HTLV-1 orf-I encoded proteins in viral transmission and persistence

Fig. 1

Structure of orf-I proteins p12 and p8. Amino acid sequence and putative functional domains of full length orf-I protein. The p12 protein is highly hydrophobic and contains an amino terminus noncanonical ER retention/retrieval motif (in bold), four putative proline-rich (PxxP) Src homology 3 (SH3)-binding domains, two putative leucine zipper (LZ) motifs, and an IL-2R β and γ chain binding motif (in blue boxes). The calcineurin-binding motif [70PSLP(I/L)T75] is indicated by a green box, and two transmembrane helices TM-1 and TM-2 domains are designated by black bars above the sequence. The black triangles indicate the two cleavage sites between amino acid positions 9 and 10, and 29 and 30, respectively. The asterisk denotes the position of cysteine 39. The proteolytic cleavage site G29/L30 leading to the production of p8 is indicated with a red arrow. The lysine-to-arginine variant is highlighted at position 88 by a red box. Arginine at this position increases the stability of the protein

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