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1f2q
From Proteopedia
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|PDB= 1f2q |SIZE=350|CAPTION= <scene name='initialview01'>1f2q</scene>, resolution 2.40Å | |PDB= 1f2q |SIZE=350|CAPTION= <scene name='initialview01'>1f2q</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2q OCA], [http://www.ebi.ac.uk/pdbsum/1f2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f2q RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Jardetzky, T S.]] | [[Category: Jardetzky, T S.]] | ||
[[Category: Kinet, J P.]] | [[Category: Kinet, J P.]] | ||
| - | [[Category: NAG]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
[[Category: ige-binding protein]] | [[Category: ige-binding protein]] | ||
| Line 31: | Line 33: | ||
[[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 Sun Mar 30 20:14:34 2008'' |
Revision as of 17:14, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 20:14:34 2008
