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2brs
From Proteopedia
| 2brs, resolution 2.20Å () | |||||||||
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| Sites: | |||||||||
| Ligands: | |||||||||
| Non-Standard Residues: | , | ||||||||
| Domains: | CLECT_EMBP_like | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
EMBP HEPARIN COMPLEX
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2BRS is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR. Eosinophil-granule major basic protein, a C-type lectin, binds heparin. Biochemistry. 2005 Nov 1;44(43):14152-8. PMID:16245931 doi:10.1021/bi051112b
Page seeded by OCA on Tue Feb 17 08:57:11 2009
