Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
The cAMP receptor protein (CRP) of Escherichia coli is a dimer of a two-domain subunit. It requires binding of cAMP for a conformational change in order to function as a site-specific DNA-binding protein that regulates gene activity. The hinge region connecting the cAMP-binding domain to the DNA-bin...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1992
|
| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC50200/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1409686/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.20.9700 |
| Tagy: |
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|