1h8u
From Proteopedia
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|PDB= 1h8u |SIZE=350|CAPTION= <scene name='initialview01'>1h8u</scene>, resolution 1.80Å | |PDB= 1h8u |SIZE=350|CAPTION= <scene name='initialview01'>1h8u</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8u OCA], [http://www.ebi.ac.uk/pdbsum/1h8u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h8u RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Chronic infections, due to MBL deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Diabetes mellitus, gestational, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Mannose-binding protein deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Meningococcal disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Swaminathan, G J.]] | [[Category: Swaminathan, G J.]] | ||
[[Category: Weaver, A J.]] | [[Category: Weaver, A J.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: embp]] | [[Category: embp]] | ||
[[Category: eosinophil granule protein]] | [[Category: eosinophil granule protein]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:08 2008'' |
Revision as of 18:00, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE EOSINOPHIL MAJOR BASIC PROTEIN AT 1.8A: AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY
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.
About this Structure
1H8U is a Single protein structure of sequence from Homo sapiens. 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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