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PDBsum entry 4j4p
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Immune system
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PDB id
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4j4p
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Contents |
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315 a.a.
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224 a.a.
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215 a.a.
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PDB id:
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| Name: |
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Immune system
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Title:
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The complex of human ige-fc with two bound fab fragments
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Structure:
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Ig epsilon chain c region. Chain: a, b. Engineered: yes. Mutation: yes. Immunoglobulin g fab fragment heavy chain. Chain: h, c. Engineered: yes. Immunoglobulin g fab fragment light chain. Chain: l, d.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ighe. Expressed in: mus musculus. Expression_system_taxid: 10090. Expressed in: cricetulus griseus. Expression_system_taxid: 10029.
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Resolution:
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2.91Å
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R-factor:
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0.239
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R-free:
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0.284
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Authors:
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N.Drinkwater,B.J.Sutton
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Key ref:
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N.Drinkwater
et al.
(2014).
Human immunoglobulin E flexes between acutely bent and extended conformations.
Nat Struct Biol,
21,
397-404.
PubMed id:
DOI:
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Date:
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07-Feb-13
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Release date:
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12-Mar-14
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PROCHECK
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Headers
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References
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P01854
(IGHE_HUMAN) -
Immunoglobulin heavy constant epsilon from Homo sapiens
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Seq:
Struc:
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546 a.a.
315 a.a.*
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DOI no:
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Nat Struct Biol
21:397-404
(2014)
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PubMed id:
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Human immunoglobulin E flexes between acutely bent and extended conformations.
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N.Drinkwater,
B.P.Cossins,
A.H.Keeble,
M.Wright,
K.Cain,
H.Hailu,
A.Oxbrow,
J.Delgado,
L.K.Shuttleworth,
M.W.Kao,
J.M.McDonnell,
A.J.Beavil,
A.J.Henry,
B.J.Sutton.
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ABSTRACT
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Crystallographic and solution studies have shown that IgE molecules are acutely
bent in their Fc region. Crystal structures reveal the Cɛ2 domain pair folded
back onto the Cɛ3-Cɛ4 domains, but is the molecule exclusively bent or can the
Cɛ2 domains adopt extended conformations and even 'flip' from one side of the
molecule to the other? We report the crystal structure of IgE-Fc captured in a
fully extended, symmetrical conformation and show by molecular dynamics,
calorimetry, stopped-flow kinetic, surface plasmon resonance (SPR) and Förster
resonance energy transfer (FRET) analyses that the antibody can indeed adopt
such extended conformations in solution. This diversity of conformational states
available to IgE-Fc offers a new perspective on IgE function in allergen
recognition, as part of the B-cell receptor and as a therapeutic target in
allergic disease.
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Links
