Fig. 3.
Fig. 3. Alignment of mouse and human Lutheran glycoprotein sequences. / Identical amino acid residues and conservative substitutions (+) between the mouse and human sequences are indicated. Residues are numbered from the known N-terminal residue in human Lu gp. The 2 cysteine residues (*) within each of the 5 predicted IgSF domains are conserved. Potential N-glycosylation sites are boxed—3 of the 4 sites in the mouse sequence are conserved. The proline-rich, putative SH3-binding site within the cytoplasmic domain of human Lu gp is underlined—this motif is partly conserved in the mouse sequence. D1-D5 indicates 5 extracellular, IgSF domains; TM, transmembrane region. The cDNA and translated amino acid sequences have been submitted to GenBank (accession number AF221507).

Alignment of mouse and human Lutheran glycoprotein sequences.

Identical amino acid residues and conservative substitutions (+) between the mouse and human sequences are indicated. Residues are numbered from the known N-terminal residue in human Lu gp. The 2 cysteine residues (*) within each of the 5 predicted IgSF domains are conserved. Potential N-glycosylation sites are boxed—3 of the 4 sites in the mouse sequence are conserved. The proline-rich, putative SH3-binding site within the cytoplasmic domain of human Lu gp is underlined—this motif is partly conserved in the mouse sequence. D1-D5 indicates 5 extracellular, IgSF domains; TM, transmembrane region. The cDNA and translated amino acid sequences have been submitted to GenBank (accession number AF221507).

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