| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-65 |
Sentence |
denotes |
Crystal structure of the eosinophil major basic protein at 1.8 A. |
| T2 |
66-122 |
Sentence |
denotes |
An atypical lectin with a paradigm shift in specificity. |
| T3 |
123-254 |
Sentence |
denotes |
The eosinophil major basic protein (EMBP) is the predominant constituent of the crystalline core of the eosinophil primary granule. |
| T4 |
255-376 |
Sentence |
denotes |
EMBP is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases such as asthma. |
| T5 |
377-605 |
Sentence |
denotes |
Here we report the crystal structure of EMBP at 1.8 A resolution, and show that it is similar to that of members of the C-type lectin superfamily with which it shares minimal amino acid sequence identity (approximately 15--28%). |
| T6 |
606-669 |
Sentence |
denotes |
However, this protein lacks a Ca(2+)/carbohydrate-binding site. |
| T7 |
670-729 |
Sentence |
denotes |
Our analysis suggests that EMBP specifically binds heparin. |
| T8 |
730-860 |
Sentence |
denotes |
Based on our results, we propose a possible new function for this protein, which is likely to have implications for EMBP function. |
