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1f2q
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Allergic responses result from the activation of mast cells by the human | + | 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== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Garman, S | + | [[Category: Garman, S C.]] |
| - | [[Category: Jardetzky, T | + | [[Category: Jardetzky, T S.]] |
| - | [[Category: Kinet, J | + | [[Category: Kinet, J P.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:12 2008'' |
Revision as of 10:34, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 12:34:12 2008
