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Phosphorylation of the IDP KID modulates affinity for KIX by increasing the lifetime of the complex

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 ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.bpj.2017.10.015

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
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

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