Figure 1

Analysis of the conserved regions of BLV and HTLV-1 TM. (A) Alignment of the BLV and HTLV-1 TM sequences, the predicted coiled coil of BLV TM is indicated between the arrow heads; the LHR is in bold; the helical regions of the HTLV-1 TM are boxed; the limits of the HTLV-1 crystal structure are marked by asters; and the membrane spanning region is underlined. (B) The HTLV-1 core coiled-coil and, on the right, the leash and α-helical region that is mimicked by the HTLV-1 inhibitory peptide (from PDB 1MG1). The face of the peptide that interacts with the coiled coil is shown. For the sequence alignment and structural renderings, residues identical between BLV and HTLV-1 are shown in red, conservative substitutions are blue, and non-conserved are rendered white. Amino acid coordinates refer to the full-length envelope precursor. (C) Detail of the predicted interaction of the HTLV-1 LHR-mimetic peptide (ribbon structure) with the surface of the coiled coil (space filling form) based on the structure of Kobe et al. [16]; shading as above.