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Interleukin-2 signalling is modulated by a labile disulfide bond in the CD132 chain of its receptor.

Abstract:

Certain disulfide bonds present in leucocyte membrane proteins are labile and can be reduced in inflammation. This can cause structural changes that result in downstream functional effects, for example, in integrin activation. Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokines including interleukin-2 and interleukin-4 (IL-2 and IL-4). The Cys(183)-Cys(232) disulfide bond in...

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Publication status:
Published

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Publisher copy:
10.1098/rsob.110036

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
Open biology
Volume:
2
Issue:
1
Pages:
110036
Publication date:
2012-01-01
DOI:
EISSN:
2046-2441
ISSN:
2046-2441
Source identifiers:
228588

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