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Title:

The molecular basis of chaperone-mediated interleukin 23 assembly control.

Document type:
Article; Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Meier, Susanne; Bohnacker, Sina; Klose, Carolin J; Lopez, Abraham; Choe, Christian A; Schmid, Philipp W N; Bloemeke, Nicolas; Rührnößl, Florian; Haslbeck, Martin; Bieren, Julia Esser-von; Sattler, Michael; Huang, Po-Ssu; Feige, Matthias J
Abstract:
The functionality of most secreted proteins depends on their assembly into a defined quaternary structure. Despite this, it remains unclear how cells discriminate unassembled proteins en route to the native state from misfolded ones that need to be degraded. Here we show how chaperones can regulate and control assembly of heterodimeric proteins, using interleukin 23 (IL-23) as a model. We find that the IL-23 α-subunit remains partially unstructured until assembly with its β-subunit occurs and id...     »
Journal title abbreviation:
Nat Commun
Year:
2019
Journal volume:
10
Journal issue:
1
Fulltext / DOI:
doi:10.1038/s41467-019-12006-x
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/31511508
Print-ISSN:
2041-1723
TUM Institution:
Molekulare Allergologie (Prof. Schmidt-Weber)
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