| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-112 |
Sentence |
denotes |
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. |
| T1 |
0-112 |
Sentence |
denotes |
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. |
| T2 |
113-322 |
Sentence |
denotes |
S-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. |
| T2 |
113-322 |
Sentence |
denotes |
S-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. |
| T3 |
323-495 |
Sentence |
denotes |
We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. |
| T3 |
323-495 |
Sentence |
denotes |
We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. |
| T4 |
496-620 |
Sentence |
denotes |
The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. |
| T4 |
496-620 |
Sentence |
denotes |
The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. |
| T5 |
621-826 |
Sentence |
denotes |
Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. |
| T5 |
621-826 |
Sentence |
denotes |
Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. |
| T6 |
827-952 |
Sentence |
denotes |
Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. |
| T6 |
827-952 |
Sentence |
denotes |
Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. |
| T7 |
953-1065 |
Sentence |
denotes |
These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins. |
| T7 |
953-1065 |
Sentence |
denotes |
These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins. |