2brs | pdb_00002brs
EMBP HEPARIN COMPLEX
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| 2brs, resolution 2.20Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | IDU, SGN, SO4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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 Ca(2+)- 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 Ca(2+), 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.
About this Structure
2BRS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Eosinophil-granule major basic protein, a C-type lectin, binds heparin., Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR, Biochemistry. 2005 Nov 1;44(43):14152-8. PMID:16245931
Page seeded by OCA on Mon Mar 31 02:10:49 2008
