- Abstract:
-
Intrinsically disordered proteins (IDPs) are known to undergo a range of posttranslational modifications, but by what mechanism do such modifications affect the binding of an IDP to its partner protein? We investigate this question using one such IDP, the kinase inducible domain (KID) of the transcription factor CREB, which interacts with the KIX domain of CREB-binding protein upon phosphorylation. As with many other IDPs, KID undergoes coupled folding and binding to form α-helical structure ...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Publisher copy:
- 10.1016/j.bpj.2017.10.015
-
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- Publisher:
- Elsevier Publisher's website
- Journal:
- Biophysical Journal Journal website
- Volume:
- 113
- Issue:
- 12
- Pages:
- 2706-2712
- Publication date:
- 2017-12-19
- Acceptance date:
- 2017-10-10
- DOI:
- EISSN:
-
1542-0086
- ISSN:
-
0006-3495
- Pubs id:
-
pubs:867845
- URN:
-
uri:981e5fe9-1a20-427a-9315-f34a1f1691db
- UUID:
-
uuid:981e5fe9-1a20-427a-9315-f34a1f1691db
- Local pid:
- pubs:867845
- Language:
- English
- Keywords:
- Copyright holder:
- Biophysical Society
- Copyright date:
- 2017
- Notes:
- © 2017 Biophysical Society. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- License:
- CC BY
Journal article
Phosphorylation of the IDP KID modulates affinity for KIX by increasing the lifetime of the complex
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