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. 1997 Apr 15;94(8):3644–3649. doi: 10.1073/pnas.94.8.3644

Figure 4.

Figure 4

(A) Schematic representation of all the potential CNBr (open arrows) and Lys-C (solid arrows) cleavage sites within the hPTH/PTHrP receptor sequence that are glycosylated and within the the molecular size range of the largest observed CNBr-generated fragment IB (≈46 kDa). Y represents the position of the four conserved N-linked glycosylation sites. (B) Schematic representation of a membrane-embedded portion of the hPTH/PTHrP receptor (amino-acids 166–254). The agonist-binding receptor domain Phe173–Met189 (shaded circles), identified in this report, is shown. Undetailed structures of the first and second transmembrane (TM) helical domains and the first cytoplasmic loop are included. Y represents putative N-linked glycosylation sites, and open circles represent amino acids.