1o0v

From Proteopedia

Revision as of 14:31, 15 February 2008

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

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