1o0v

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|PDB= 1o0v |SIZE=350|CAPTION= <scene name='initialview01'>1o0v</scene>, resolution 2.6&Aring;
|PDB= 1o0v |SIZE=350|CAPTION= <scene name='initialview01'>1o0v</scene>, resolution 2.6&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= IgE(ND) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= IgE(ND) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0v OCA], [http://www.ebi.ac.uk/pdbsum/1o0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o0v RCSB]</span>
}}
}}
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[[Category: Wan, T.]]
[[Category: Wan, T.]]
[[Category: Young, R J.]]
[[Category: Young, R J.]]
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[[Category: GOL]]
 
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[[Category: SO4]]
 
[[Category: ige fc]]
[[Category: ige fc]]
[[Category: immunoglobulin e]]
[[Category: immunoglobulin e]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:04:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:38:17 2008''

Revision as of 19:38, 30 March 2008


PDB ID 1o0v

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: , , , ,
Gene: IgE(ND) (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The crystal structure of IgE Fc reveals an asymmetrically bent conformation


Overview

The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells.

About this Structure

1O0V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of IgE Fc reveals an asymmetrically bent conformation., Wan T, Beavil RL, Fabiane SM, Beavil AJ, Sohi MK, Keown M, Young RJ, Henry AJ, Owens RJ, Gould HJ, Sutton BJ, Nat Immunol. 2002 Jul;3(7):681-6. Epub 2002 Jun 17. PMID:12068291

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