1O0V

The crystal structure of IgE Fc reveals an asymmetrically bent conformation

Replaces:  1LS0

Summary for 1O0V

• Entry DOI: 10.2210/pdb1o0v/pdb
• Descriptor: Immunoglobulin heavy chain epsilon-1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: ige fc, immunoglobulin e, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 75716.17

Authors

Wan, T.,Beavil, R.L.,Fabiane, S.M.,Beavil, A.J.,Sohi, M.K.,Keown, M.,Young, R.J.,Henry, A.J.,Owens, R.J.,Gould, H.J.,Sutton, B.J. (deposition date: 2002-09-06, release date: 2002-09-18, Last modification date: 2024-10-30)

Primary citation

Wan, T.,Beavil, R.L.,Fabiane, S.M.,Beavil, A.J.,Sohi, M.K.,Keown, M.,Young, R.J.,Henry, A.J.,Owens, R.J.,Gould, H.J.,Sutton, B.J.
The crystal structure of IgE Fc reveals an asymmetrically bent conformation
NAT.IMMUNOL., 3:681-686, 2002

PubMed Abstract: 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.

PubMed: 12068291
DOI: 10.1038/ni811

Experimental method

X-RAY DIFFRACTION (2.6 Å)