Ca2+-dependent Structural Changes in the B-cell Receptor CD23 Increase Its Affinity for Human Immunoglobulin E (Q27678651)

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3 March 2020

title

Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin E (English)

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3 March 2020

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2

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3 March 2020

Hannah J Gould

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James M. McDonnell

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3 March 2020

Andrew J. Beavil

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Balvinder Dhaliwal

9

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1

Daopeng Yuan

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3 March 2020

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Stella Fabiane

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author name string

Richard G Hibbert

3

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3 March 2020

Brian J Sutton

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language of work or name

English

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publication date

17 June 2013

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Journal of Biological Chemistry

3 March 2020

published in

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volume

288

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issue

30

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page(s)

21667-21677

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Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor Fc RI

3 March 2020

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21 January 2018

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21 January 2018

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Interaction of the Low-Affinity Receptor CD23/FcεRII Lectin Domain with the Fcε3−4 Fragment of Human Immunoglobulin E†

21 January 2018

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Production of a chimeric form of CD23 that is oligomeric and blocks IgE binding to the Fc epsilonRI.

21 January 2018

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12 December 2020

Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding

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12 December 2020

ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23

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12 December 2020

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Identifiers

DOI

10.1074/JBC.M113.480657

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23775083%20AND%20SRC:MED&resulttype=core&format=json

3 March 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23775083%20AND%20SRC:MED&resulttype=core&format=json

3 March 2020

PubMed publication ID

23775083

1 reference