1f2q

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(New page: 200px<br /> <applet load="1f2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2q, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1f2q.gif|left|200px]]<br />
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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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<applet load="1f2q" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1f2q, resolution 2.40&Aring;" />
caption="1f2q, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR'''<br />
'''CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR'''<br />
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==About this Structure==
==About this Structure==
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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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F2Q OCA].
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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].
==Reference==
==Reference==
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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:48:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:45:24 2008''

Revision as of 13:45, 15 February 2008


1f2q, resolution 2.40Å

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CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

Overview

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.

About this Structure

1F2Q is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

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

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