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. 2000 Feb;11(2):765–772. doi: 10.1091/mbc.11.2.765

Figure 1.

Figure 1

HA-RAP and HA-RAP (Tm−) chimeras. (A) Linear structure of X31 HA(WT). The positions of the two major disulfide bonds (C52–277C and C14–466C) and the transmembrane domain (514–540) are numbered on the right of the molecule, the positions of the glycosylation sites are numbered on the left of the molecule. The mature HA contains a total of 550 amino acid residues. (B) Structure of HA-RAP fusion protein. Two hundred ninety-eight amino residues (residues 25–322) of RAP were fused to the cytosolic tail of HA. There is a FLAG tag at the very C-terminal end. The mature HA-RAP protein contains 856 amino acid residues. (C) Structure of HA-RAP (Tm−). This protein differs from the HA-RAP fusion protein in that the transmembrane domain and cytosolic tail from wild-type HA are absent. The mature HA-RAP (Tm−) contains 819 amino acid residues.