Journal article
Self-organization and regulation of intrinsically disordered proteins with folded N-termini
- Abstract:
- Here we hypothesize that some proteins use their structured N-terminal domains (SNTDs) to organize the remaining protein chain by means of intramolecular interactions, so generating partially condensed proteins. This model has several attractive features: as the nascent protein chain emerges from the ribosome, the SNTD folds spontaneously and then serves as a nucleation point for the yet unstructured amino acid chain, creating more compact shapes. This reduces the risk of protein degradation or aggregation. Moreover, an interspersed pattern of SNTD-docked regions and free loops can coordinate assembly of sub-complexes in defined loop-sections and enables novel regulatory mechanisms, for example through posttranslational modifications of docked regions.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 195.6KB, Terms of use)
-
- Publisher copy:
- 10.1371/journal.pbio.1000591
Authors
- Publisher:
- Public Library of Science
- Journal:
- PLoS Biology More from this journal
- Volume:
- 9
- Issue:
- 2
- Pages:
- ARTN e1000591
- Publication date:
- 2011-02-15
- DOI:
- EISSN:
-
1545-7885
- ISSN:
-
1544-9173
- Language:
-
English
- Keywords:
- Pubs id:
-
179128
- UUID:
-
uuid:01042d19-5aa3-4c3b-99db-2467efd3140b
- Local pid:
-
pubs:179128
- Source identifiers:
-
179128
- Deposit date:
-
2012-12-19
- ARK identifier:
Terms of use
- Copyright holder:
- Simister et al
- Copyright date:
- 2011
- Notes:
- Copyright: © 2011 Simister et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record