期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 28, 页码 26197-26203出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M100848200
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资金
- NIAID NIH HHS [AI 25230, AI 09728] Funding Source: Medline
The eosinophil major basic protein (EMBP) is the predominant constituent of the crystalline core of the eosinophil primary granule. EMBP is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases such as asthma, Here we report the crystal structure of EMBP at 1.8 Angstrom 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 (similar to 15-28%). However, this protein lacks a Ca2+/carbohydrate-binding site. Our analysis suggests that EMBP specifically binds heparin, Based on our results, we propose a possible new function for this protein, which is likely to have implications for EMBP function.
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