| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-137 |
Sentence |
denotes |
Structural and thermodynamic insights into chitooligosaccharide binding to human cartilage chitinase 3-like protein 2 (CHI3L2 or YKL-39). |
| T2 |
138-243 |
Sentence |
denotes |
Four crystal structures of human YKL-39 were solved in the absence and presence of chitooligosaccharides. |
| T3 |
244-369 |
Sentence |
denotes |
The structure of YKL-39 comprises a major (β/α)8 triose-phosphate isomerase barrel domain and a small α + β insertion domain. |
| T4 |
370-504 |
Sentence |
denotes |
Structural analysis demonstrates that YKL-39 interacts with chitooligosaccharides through hydrogen bonds and hydrophobic interactions. |
| T5 |
505-604 |
Sentence |
denotes |
The binding of chitin fragments induces local conformational changes that facilitate tight binding. |
| T6 |
605-872 |
Sentence |
denotes |
Compared with other GH-18 members, YKL-39 has the least extended chitin-binding cleft, containing five subsites for sugars, namely (-3)(-2)(-1)(+1)(+2), with Trp-360 playing a prominent role in the sugar-protein interactions at the center of the chitin-binding cleft. |
| T7 |
873-1159 |
Sentence |
denotes |
Evaluation of binding affinities obtained from isothermal titration calorimetry and intrinsic fluorescence spectroscopy suggests that YKL-39 binds to chitooligosaccharides with Kd values in the micromolar concentration range and that the binding energies increase with the chain length. |
| T8 |
1160-1328 |
Sentence |
denotes |
There were no significant differences between the Kd values of chitopentaose and chitohexaose, supporting the structural evidence for the five binding subsite topology. |
| T9 |
1329-1438 |
Sentence |
denotes |
Thermodynamic analysis indicates that binding of chitooligosaccharide to YKL-39 is mainly driven by enthalpy. |
