2ige

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:2ige.png|left|200px]]
 
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==THE NATURE AND IMPORTANCE OF THE INTER-EPSILON CHAIN DISULPHIDE BONDS IN HUMAN IGE==
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The line below this paragraph, containing "STRUCTURE_2ige", creates the "Structure Box" on the page.
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<StructureSection load='2ige' size='340' side='right'caption='[[2ige]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ige FirstGlance], [https://www.ebi.ac.uk/pdbsum/2ige PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ige ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2ige| PDB=2ige | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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IgE antibodies are best known for their pathological role in allergy. The class-specific effector sites are located in the epsilon chains; these form covalent dimers via two cystine residues (Cys241 and Cys328) linking opposite C epsilon 2 domains. The nature and biological significance of the inter-epsilon chain disulfide-bond arrangement is unresolved. For structural and functional analysis site-specific mutations were introduced into the C epsilon 2 domain of recombinant human IgE. The introduction of an additional cyanogen bromide cleavage site (His246----Met) facilitated the identification of parallel disulfide bond pairing. This linkage was also confirmed for myeloma IgE PS by sequence determination of disulfide-linked C epsilon 2 dimers. Substitution of Cys241 and Cys328 by Ser does not destroy receptor binding, but reductive alkylation, or the replacement of Cys328 by Met, leads to loss of activity. This shows that covalent dimerization is not essential for IgE/receptor interaction and points to the importance of the structural integrity of the site surrounding Cys328, visualized in a new model of human Fc epsilon.
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===THE NATURE AND IMPORTANCE OF THE INTER-EPSILON CHAIN DISULPHIDE BONDS IN HUMAN IGE===
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The nature and importance of the inter-epsilon chain disulfide bonds in human IgE.,Helm BA, Ling Y, Teale C, Padlan EA, Bruggemann M Eur J Immunol. 1991 Jun;21(6):1543-8. PMID:1828428<ref>PMID:1828428</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_1828428}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2ige" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 1828428 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_1828428}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGE OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:1828428</ref><references group="xtra"/>
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[[Category: Helm, B A]]
[[Category: Helm, B A]]
[[Category: Padlan, E A]]
[[Category: Padlan, E A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:45:27 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THE NATURE AND IMPORTANCE OF THE INTER-EPSILON CHAIN DISULPHIDE BONDS IN HUMAN IGE

PDB ID 2ige

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