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Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex
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 transcr...
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| Vydáno v: | Biophys J |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
The Biophysical Society
2017
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5770967/ https://ncbi.nlm.nih.gov/pubmed/29262363 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2017.10.015 |
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