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1f2q
From Proteopedia
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| - | [[Image:1f2q.jpg|left|200px]] | + | [[Image:1f2q.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR''' | + | {{Structure |
| + | |PDB= 1f2q |SIZE=350|CAPTION= <scene name='initialview01'>1f2q</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F2Q is a [ | + | 1F2Q is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/9875849 9875849] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:36 2008'' |
Revision as of 09:03, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 11:03:36 2008
