期刊
BIOCHEMISTRY
卷 44, 期 43, 页码 14152-14158出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi051112b
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资金
- NIAID NIH HHS [AI09728] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
The eosinophil major basic protein (EMBP), a constituent of the eosinophil secondary granule, is implicated in cytotoxicity and mediation of allergic disorders such as asthma. It is a member of the C-type lectin family, but lacks a Ca2+- and carbohydrate-binding site as seen in other members of this family. Here, we report the crystal structure of EMBP in complex with a heparin disaccharide and in the absence of Ca2+, the first such report of any C-lectin with this sugar. We also provide direct evidence of binding of EMBP to heparin and heparin disaccharide by surface plasmon resonance. We propose that the sugars recognized by EMBP are likely to be proteoglycans such as heparin, leading to new interpretations for EMBP function.
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