1f2q

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[[Image:1f2q.jpg|left|200px]]<br /><applet load="1f2q" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f2q, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR==
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Allergic responses result from the activation of mast cells by the human, high-affinity IgE receptor. IgE-mediated allergic reactions may develop to, a variety of environmental compounds, but the initiation of a response, requires the binding of IgE to its high-affinity receptor. We have solved, the X-ray crystal structure of the antibody-binding domains of the human, IgE receptor at 2.4 A resolution. The structure reveals a highly bent, arrangement of immunoglobulin domains that form an extended convex surface, of interaction with IgE. A prominent loop that confers specificity for IgE, molecules extends from the receptor surface near an unusual arrangement of, four exposed tryptophans. The crystal structure of the IgE receptor, provides a foundation for the development of new therapeutic approaches to, allergy treatment.
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<StructureSection load='1f2q' size='340' side='right'caption='[[1f2q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f2q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2Q FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2q OCA], [https://pdbe.org/1f2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2q RCSB], [https://www.ebi.ac.uk/pdbsum/1f2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FCERA_HUMAN FCERA_HUMAN] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/1f2q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f2q ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution. The structure reveals a highly bent arrangement of immunoglobulin domains that form an extended convex surface of interaction with IgE. A prominent loop that confers specificity for IgE molecules extends from the receptor surface near an unusual arrangement of four exposed tryptophans. The crystal structure of the IgE receptor provides a foundation for the development of new therapeutic approaches to allergy treatment.
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==About this Structure==
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Crystal structure of the human high-affinity IgE receptor.,Garman SC, Kinet JP, Jardetzky TS Cell. 1998 Dec 23;95(7):951-61. PMID:9875849<ref>PMID:9875849</ref>
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1F2Q 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=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2Q OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the human high-affinity IgE receptor., Garman SC, Kinet JP, Jardetzky TS, Cell. 1998 Dec 23;95(7):951-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9875849 9875849]
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</div>
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<div class="pdbe-citations 1f2q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Garman, S.C.]]
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[[Category: Garman SC]]
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[[Category: Jardetzky, T.S.]]
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[[Category: Jardetzky TS]]
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[[Category: Kinet, J.P.]]
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[[Category: Kinet JP]]
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[[Category: NAG]]
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[[Category: glycoprotein]]
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[[Category: ige-binding protein]]
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[[Category: immunoglobulin fold]]
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[[Category: receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:45:24 2008''
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Current revision

CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

PDB ID 1f2q

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