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 1.80&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1h8u.gif|left|200px]]<br /><applet load="1h8u" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1h8u" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1h8u, resolution 1.80&Aring;" />
caption="1h8u, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF THE EOSINOPHIL MAJOR BASIC PROTEIN AT 1.8A: AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY'''<br />
'''CRYSTAL STRUCTURE OF THE EOSINOPHIL MAJOR BASIC PROTEIN AT 1.8A: AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY'''<br />
==Overview==
==Overview==
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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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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==
==Disease==
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==About this Structure==
==About this Structure==
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1H8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H8U OCA].
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1H8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8U OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Acharya, K.R.]]
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[[Category: Acharya, K R.]]
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[[Category: Checkel, J.L.]]
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[[Category: Checkel, J L.]]
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[[Category: Gleich, G.J.]]
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[[Category: Gleich, G J.]]
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[[Category: Leonidas, D.D.]]
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[[Category: Leonidas, D D.]]
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[[Category: Loegering, D.A.]]
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[[Category: Loegering, D A.]]
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[[Category: Swaminathan, G.J.]]
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[[Category: Swaminathan, G J.]]
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[[Category: Weaver, A.J.]]
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[[Category: Weaver, A J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:14:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:39 2008''

Revision as of 10:58, 21 February 2008


1h8u, resolution 1.80Å

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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 and 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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