1h8u
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(New page: 200px<br /> <applet load="1h8u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h8u, resolution 1.80Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:07, 12 November 2007
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CRYSTAL STRUCTURE OF THE EOSINOPHIL MAJOR BASIC PROTEIN AT 1.8A: AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Chronic infections, due to MBL deficiency OMIM:[154545], Diabetes mellitus, gestational, susceptibility to OMIM:[154545], Mannose-binding protein deficiency OMIM:[154545], Meningococcal disease, susceptibility to OMIM:[154545]
About this Structure
1H8U is a Single protein structure of sequence from Homo sapiens with SO4 and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity., Swaminathan GJ, Weaver AJ, Loegering DA, Checkel JL, Leonidas DD, Gleich GJ, Acharya KR, J Biol Chem. 2001 Jul 13;276(28):26197-203. Epub 2001 Apr 23. PMID:11319227
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