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The KDEL trafficking receptor exploits pH to tune the strength of an unusual short hydrogen bond

Abstract:

The endoplasmic reticulum (ER) is the main site of protein synthesis in eukaryotic cells and requires a high concentration of luminal chaperones to function. During protein synthesis, ER luminal chaperones are swept along the secretory pathway and must be retrieved to maintain cell viability. ER protein retrieval is achieved by the KDEL receptor, which recognises a C-terminal Lys-Asp-Glu-Leu (KDEL) sequence. Recognition of ER proteins by the KDEL receptor is pH dependent, with binding occurri...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41598-020-73906-3

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0000-0001-5100-8836
Publisher:
Springer Nature
Journal:
Scientific Reports More from this journal
Volume:
10
Issue:
1
Article number:
16903
Publication date:
2020-10-09
Acceptance date:
2020-09-23
DOI:
EISSN:
2045-2322
Language:
English
Keywords:
Pubs id:
1137157
Local pid:
pubs:1137157
Deposit date:
2020-10-12

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