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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI
Authors
A Vagin
A Whitty
+64 more
AA Vaguine
AJ Beavil
AJ Henry
AJ Henry
Andrew J Beavil
Anna M Davies
AT Brünger
BA Wurzburg
BA Wurzburg
Balvinder Dhaliwal
Brian J Sutton
DG Myszka
E Hodis
E Krissinel
EF Pettersen
Enrico Girardi
Hannah J Gould
HJ Gould
HJ Gould
IW Davis
J Hunt
J Hunt
J Painter
J Rouvinen
James Hunt
James M McDonnell
JE Nettleship
JM McDonnell
JM McDonnell
JN Arnold
Joanne E Nettleship
JPD Cook
K Maenaka
KH Roux
KJ Dorrington
L Vangelista
M Basu
M Li
M Niemi
Mary D Holdom
MI Asher
MS Weiss
NE Price
O Mirza
P Emsley
P Sondermann
P Sondermann
Ray J Owens
RJ Young
S Hayward
S Hayward
S Holgate
S Padavattan
S Padavattan
S Radaev
S Wlodek
Sarah C Bagby
SC Garman
SC Garman
SC Garman
SJ Demarest
T Wan
Y Zheng
Z Otwinowski
Publication date
1 January 2011
Publisher
'Springer Science and Business Media LLC'
Doi
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on
PubMed
Abstract
Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcI RI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Ã.-resolution crystal structure of human IgE-Fc (consisting of the CI 2, CI 3 and CI 4 domains) bound to the extracellular domains of the FcI RI Î ± chain. Comparison with the structure of free IgE-Fc (reported here at a resolution of 1.9 Ã.) shows that the antibody, which has a compact, bent structure before receptor engagement, becomes even more acutely bent in the complex. Thermodynamic analysis indicates that the interaction is entropically driven, which explains how the noncontacting CI 2 domains, in place of the flexible hinge region of IgG antibodies, contribute together with the conformational changes to the unique binding properties of IgE. © 2011 Nature America, Inc. All rights reserved
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