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Conserved helix-flanking prolines modulate intrinsically disordered protein: target affinity by altering the lifetime of the bound complex

Abstract:

Appropriate integration of cellular signals requires a delicate balance of ligand-target binding affinities. Increasing the level of residual structure in intrinsically disordered proteins (IDPs), which are overrepresented in these cellular processes, has been shown previously to enhance binding affinities and alter cellular function. Conserved proline residues are commonly found flanking regions of IDPs that become helical upon interacting with a partner protein. Here, we mutate these helix-...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acs.biochem.7b00179

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Role:
Author
ORCID:
0000-0003-1466-4011
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Funding agency for:
Daughdrill, GW
Grant:
1R01GM115556-01A1
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Funding agency for:
Clarke, J
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Publisher:
American Chemical Society Publisher's website
Journal:
Biochemistry Journal website
Volume:
56
Issue:
18
Pages:
2379–2384
Publication date:
2017-04-20
Acceptance date:
2017-04-13
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Pmid:
28425697
Source identifiers:
697224

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