| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-103 |
Sentence |
denotes |
A putative selectivity filter in the G-protein-coupled receptors for parathyroid hormone and secretion. |
| T1 |
0-103 |
Sentence |
denotes |
A putative selectivity filter in the G-protein-coupled receptors for parathyroid hormone and secretion. |
| TextSentencer_T2 |
104-282 |
Sentence |
denotes |
The seven transmembrane segments (TMs) of many G-protein-coupled receptors (GPCRs) are thought to form a cavity into which cognate ligands insert, leading to receptor activation. |
| T2 |
104-282 |
Sentence |
denotes |
The seven transmembrane segments (TMs) of many G-protein-coupled receptors (GPCRs) are thought to form a cavity into which cognate ligands insert, leading to receptor activation. |
| TextSentencer_T3 |
283-384 |
Sentence |
denotes |
Residues lining the cavity are often essential for optimal ligand binding and/or signal transduction. |
| T3 |
283-384 |
Sentence |
denotes |
Residues lining the cavity are often essential for optimal ligand binding and/or signal transduction. |
| TextSentencer_T4 |
385-564 |
Sentence |
denotes |
The present studies evaluated whether residues lining the cavity also contribute to specificity, using GPCRs for the polypeptides parathyroid hormone (PTH) and secretin as models. |
| T4 |
385-564 |
Sentence |
denotes |
The present studies evaluated whether residues lining the cavity also contribute to specificity, using GPCRs for the polypeptides parathyroid hormone (PTH) and secretin as models. |
| TextSentencer_T5 |
565-684 |
Sentence |
denotes |
These ligands display no sequence homology with one another, and neither ligand cross-reacts with the other's receptor. |
| T5 |
565-684 |
Sentence |
denotes |
These ligands display no sequence homology with one another, and neither ligand cross-reacts with the other's receptor. |
| TextSentencer_T6 |
685-890 |
Sentence |
denotes |
However, mutation of a single amino acid in the second TM of the secretin receptor to the corresponding residue in the PTH receptor (N192I) resulted in a receptor that binds and signals in response to PTH. |
| T6 |
685-890 |
Sentence |
denotes |
However, mutation of a single amino acid in the second TM of the secretin receptor to the corresponding residue in the PTH receptor (N192I) resulted in a receptor that binds and signals in response to PTH. |
| TextSentencer_T7 |
891-988 |
Sentence |
denotes |
The reciprocal mutation in the PTH receptor (I234N) likewise unmasked responsiveness to secretin. |
| T7 |
891-988 |
Sentence |
denotes |
The reciprocal mutation in the PTH receptor (I234N) likewise unmasked responsiveness to secretin. |
| TextSentencer_T8 |
989-1079 |
Sentence |
denotes |
Neither mutation significantly altered the response of the receptors to their own ligands. |
| T8 |
989-1079 |
Sentence |
denotes |
Neither mutation significantly altered the response of the receptors to their own ligands. |
| TextSentencer_T9 |
1080-1320 |
Sentence |
denotes |
The results suggest a model of specificity wherein TM residues near the extracellular surface of the receptor function as a selectivity filter that restricts access of inappropriate ligands to an activation site in the transmembrane cavity. |
| T9 |
1080-1320 |
Sentence |
denotes |
The results suggest a model of specificity wherein TM residues near the extracellular surface of the receptor function as a selectivity filter that restricts access of inappropriate ligands to an activation site in the transmembrane cavity. |