Figure 2
Figure 2. Schematic model of RhAG. The 2-D model shows the RhAG protein with transmembrane spans as predicted by the alignment of RhAG with NeRh50.9 The layout emphasizes the close proximity of the 2 residues associated with OHSt, Ile61 and Phe65, found in span 2 and highlighted in red. The phenylalanines that form the putative phe-gate (Phe120 and Phe225) are highlighted in yellow. The 2 highly conserved His residues (His175 and His334) are highlighted in green. Beige infill denotes residues mutated in Rhnull syndrome. Frame shift and splice site mutations have also been reported in Rhnull (reviewed in Bruce23; data not shown). Blue infill denotes blood group sites that have been assigned to RhAG very recently.24 Gray infill denotes sites susceptible to proteolytic cleavage.25 The C-terminal peptide, used in preparation of the anti-RhAG antibody, is marked by a brown line.

Schematic model of RhAG. The 2-D model shows the RhAG protein with transmembrane spans as predicted by the alignment of RhAG with NeRh50. The layout emphasizes the close proximity of the 2 residues associated with OHSt, Ile61 and Phe65, found in span 2 and highlighted in red. The phenylalanines that form the putative phe-gate (Phe120 and Phe225) are highlighted in yellow. The 2 highly conserved His residues (His175 and His334) are highlighted in green. Beige infill denotes residues mutated in Rhnull syndrome. Frame shift and splice site mutations have also been reported in Rhnull (reviewed in Bruce23 ; data not shown). Blue infill denotes blood group sites that have been assigned to RhAG very recently.24  Gray infill denotes sites susceptible to proteolytic cleavage.25  The C-terminal peptide, used in preparation of the anti-RhAG antibody, is marked by a brown line.

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