| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-75 |
Sentence |
denotes |
Characterization of the stromal cell-derived factor-1alpha-heparin complex. |
| T2 |
76-181 |
Sentence |
denotes |
The binding of chemokines to glycosaminoglycans is thought to play a crucial role in chemokine functions. |
| T3 |
182-480 |
Sentence |
denotes |
It has recently been shown that stromal cell-derived factor-1alpha (SDF-1alpha), a CXC chemokine with potent anti-human immunodeficiency virus activity, binds to heparan sulfate through a typical consensus sequence for heparin recognition (BBXB, where B is a basic residue KHLK, amino acids 24-27). |
| T4 |
481-769 |
Sentence |
denotes |
Calculation of the accessible surface, together with the electrostatic potential of the SDF-1alpha dimer, revealed that other amino acids (Arg-41 and Lys-43) are found in the same surface area and contribute to the creation of a positively charged crevice, located at the dimer interface. |
| T5 |
770-905 |
Sentence |
denotes |
GRID calculations confirmed that this binding site will be the most energetically favored area for the interaction with sulfate groups. |
| T6 |
906-1063 |
Sentence |
denotes |
Site-directed mutagenesis and surface plasmon resonance-based binding assays were used to investigate the structural basis for SDF-1alpha binding to heparin. |
| T7 |
1064-1206 |
Sentence |
denotes |
Among the residues clustered in this basic surface area, Lys-24 and Lys-27 have dominant roles and are essential for interaction with heparin. |
| T8 |
1207-1328 |
Sentence |
denotes |
Amino acids Arg-41 and Lys-43 participate in the binding but are not strictly required for the interaction to take place. |
| T9 |
1329-1547 |
Sentence |
denotes |
Direct binding assays and competition analysis with monoclonal antibodies also permitted us to show that the N-terminal residue (Lys-1), an amino acid critical for receptor activation, is involved in complex formation. |
| T10 |
1548-1846 |
Sentence |
denotes |
Binding studies with selectively desulfated heparin, heparin oligosaccharides, and heparitinase-resistant heparan sulfate fragments showed that a minimum size of 12-14 monosaccharide units is required for efficient binding and that 2-O- and N-sulfate groups have a dominant role in the interaction. |
| T11 |
1847-1971 |
Sentence |
denotes |
Finally, the heparin-binding site was identified on the crystal structure of SDF-1alpha, and a docking study was undertaken. |
| T12 |
1972-2091 |
Sentence |
denotes |
During the energy minimization process, heparin lost its perfect ribbon shape and fitted the protein surface perfectly. |
| T13 |
2092-2249 |
Sentence |
denotes |
In the model, Lys-1, Lys-24, Lys-27, and Arg-41 were found to have the major role in binding a polysaccharide fragment consisting of 13 monosaccharide units. |