Fig. 2.
(A) Schematic representation of the structure of mOSMRβ cDNA. The 5′ and 3′ UTRs (solid line) and the coding region (boxed region) containing the predicted signal sequence (hatched box) and the transmembrane domain (filled box) are shown. The position of cysteines and WS motifs that are conserved among the cytokine receptor superfamily is marked. The location of three overlapping cDNA clones isolated is also indicated. (B) Nucleotide and predicted amino acid sequence of mOSMRβ. Amino acids are shown by the one-letter code. Conserved cysteines and WS motifs are shaded. Potential asparagine-linked glycosylation sites (NXS/T) are underlined. The putative signal sequence and transmembrane domain are shown by a broken line and a double underline, respectively. Primers used to clone the cDNA are also shown as an underline with an arrow. YXXQ motifs are boxed. (C) Comparison of amino acid sequences between mOSMRβ and hOSMRβ. Identical amino acid residues are shown as bold letters.

(A) Schematic representation of the structure of mOSMRβ cDNA. The 5′ and 3′ UTRs (solid line) and the coding region (boxed region) containing the predicted signal sequence (hatched box) and the transmembrane domain (filled box) are shown. The position of cysteines and WS motifs that are conserved among the cytokine receptor superfamily is marked. The location of three overlapping cDNA clones isolated is also indicated. (B) Nucleotide and predicted amino acid sequence of mOSMRβ. Amino acids are shown by the one-letter code. Conserved cysteines and WS motifs are shaded. Potential asparagine-linked glycosylation sites (NXS/T) are underlined. The putative signal sequence and transmembrane domain are shown by a broken line and a double underline, respectively. Primers used to clone the cDNA are also shown as an underline with an arrow. YXXQ motifs are boxed. (C) Comparison of amino acid sequences between mOSMRβ and hOSMRβ. Identical amino acid residues are shown as bold letters.

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