Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-100 |
Sentence |
denotes |
Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR. |
T1 |
0-100 |
Sentence |
denotes |
Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR. |
TextSentencer_T2 |
101-300 |
Sentence |
denotes |
Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1-111) and the conserved carbohydrate recognition domain (CRD, residues 112-250). |
T2 |
101-300 |
Sentence |
denotes |
Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1-111) and the conserved carbohydrate recognition domain (CRD, residues 112-250). |
TextSentencer_T3 |
301-373 |
Sentence |
denotes |
The chimera-type galectin interacts with both glycan and peptide motifs. |
T3 |
301-373 |
Sentence |
denotes |
The chimera-type galectin interacts with both glycan and peptide motifs. |
TextSentencer_T4 |
374-493 |
Sentence |
denotes |
Complete (13)C/(15)N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible. |
T4 |
374-493 |
Sentence |
denotes |
Complete (13)C/(15)N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible. |
TextSentencer_T5 |
494-764 |
Sentence |
denotes |
Using two synthetic NT polypeptides covering residues 1-50 and 51-107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn structure from residues 18 to 32 and around PGAYP repeats. |
T5 |
494-764 |
Sentence |
denotes |
Using two synthetic NT polypeptides covering residues 1-50 and 51-107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn structure from residues 18 to 32 and around PGAYP repeats. |
TextSentencer_T6 |
765-1056 |
Sentence |
denotes |
Intramolecular interactions occur between the CRD F-face (the 5-stranded β-sheet behind the canonical carbohydrate-binding 6-stranded β-sheet of the S-face) and NT in full-length galectin-3, with the sequence P(23)GAW(26)…P(37)GASYPGAY(45) defining the primary binding epitope within the NT. |
T6 |
765-1056 |
Sentence |
denotes |
Intramolecular interactions occur between the CRD F-face (the 5-stranded β-sheet behind the canonical carbohydrate-binding 6-stranded β-sheet of the S-face) and NT in full-length galectin-3, with the sequence P(23)GAW(26)…P(37)GASYPGAY(45) defining the primary binding epitope within the NT. |
TextSentencer_T7 |
1057-1163 |
Sentence |
denotes |
Work with designed peptides indicates that the PGAX motif is crucial for self-interactions between NT/CRD. |
T7 |
1057-1163 |
Sentence |
denotes |
Work with designed peptides indicates that the PGAX motif is crucial for self-interactions between NT/CRD. |
TextSentencer_T8 |
1164-1316 |
Sentence |
denotes |
Phosphorylation at position Ser6 (and Ser12) (a physiological modification) and the influence of ligand binding have minimal effect on this interaction. |
T8 |
1164-1316 |
Sentence |
denotes |
Phosphorylation at position Ser6 (and Ser12) (a physiological modification) and the influence of ligand binding have minimal effect on this interaction. |
TextSentencer_T9 |
1317-1470 |
Sentence |
denotes |
Finally, galectin-3 molecules can interact weakly with each other via the F-faces of their CRDs, an interaction that appears to be assisted by their NTs. |
T9 |
1317-1470 |
Sentence |
denotes |
Finally, galectin-3 molecules can interact weakly with each other via the F-faces of their CRDs, an interaction that appears to be assisted by their NTs. |
TextSentencer_T10 |
1471-1597 |
Sentence |
denotes |
Overall, our results add insight to defining binding sites on galectin-3 beyond the canonical contact area for β-galactosides. |
T10 |
1471-1597 |
Sentence |
denotes |
Overall, our results add insight to defining binding sites on galectin-3 beyond the canonical contact area for β-galactosides. |