1o0v
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The distinguishing structural feature of immunoglobulin E (IgE), the | + | 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== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beavil, A | + | [[Category: Beavil, A J.]] |
| - | [[Category: Beavil, R | + | [[Category: Beavil, R L.]] |
| - | [[Category: Fabiane, S | + | [[Category: Fabiane, S M.]] |
| - | [[Category: Gould, H | + | [[Category: Gould, H J.]] |
| - | [[Category: Henry, A | + | [[Category: Henry, A J.]] |
[[Category: Keown, M.]] | [[Category: Keown, M.]] | ||
| - | [[Category: Owens, R | + | [[Category: Owens, R J.]] |
| - | [[Category: Sohi, M | + | [[Category: Sohi, M K.]] |
| - | [[Category: Sutton, B | + | [[Category: Sutton, B J.]] |
[[Category: Wan, T.]] | [[Category: Wan, T.]] | ||
| - | [[Category: Young, R | + | [[Category: Young, R J.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: immunoglobulin e]] | [[Category: immunoglobulin e]] | ||
| - | ''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 14:12:12 2008'' |
Revision as of 12:12, 21 February 2008
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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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 14:12:12 2008
Categories: Homo sapiens | Single protein | Beavil, A J. | Beavil, R L. | Fabiane, S M. | Gould, H J. | Henry, A J. | Keown, M. | Owens, R J. | Sohi, M K. | Sutton, B J. | Wan, T. | Young, R J. | GOL | SO4 | Ige fc | Immunoglobulin e
