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Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity.

Authors: Swaminathan, GJ  Weaver, AJ  Loegering, DA  Checkel, JL  Leonidas, DD  Gleich, GJ  Acharya, KR 
Citation: Swaminathan GJ, etal., J Biol Chem 2001 Jul 13;276(28):26197-203. Epub 2001 Apr 23.
Pubmed: (View Article at PubMed) PMID:11319227
DOI: Full-text: DOI:10.1074/jbc.M100848200

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 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%). However, this protein lacks a Ca(2+)/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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RGD Object Information
RGD ID: 1302346
Created: 2004-09-21
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.