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Interaction between the Prion Protein’s Copper-Bound Octarepeat Domain and a Charged C-terminal Pocket Suggests a Mechanism for N-terminal Regulation
Copper plays a critical role in prion protein (PrP) physiology. Cu(2+) binds with high affinity to the PrP N-terminal octarepeat domain (OR), and intracellular copper promotes PrP expression. The molecular details of copper coordination within the OR are now well characterized. Here we examine how C...
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| Vydáno v: | Structure |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2016
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4938727/ https://ncbi.nlm.nih.gov/pubmed/27265848 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2016.04.017 |
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