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Chapter title |
Visualizing AMPK Drug Binding Sites Through Crystallization of Full-Length Phosphorylated α2β1γ1 Heterotrimer
|
---|---|
Chapter number | 2 |
Book title |
AMPK
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Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7598-3_2 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7597-6, 978-1-4939-7598-3
|
Authors |
Christopher G. Langendorf, Jonathan S. Oakhill, Bruce E. Kemp |
Abstract |
Here, we describe the crystallization protocol for AMPK, including protein production and purification. AMPK can be readily crystallized in the presence of PEG to give diffracting crystals to a resolution of between 2.5 and 3.5 Å using synchrotron radiation. This method allows for visualization of drugs or small molecules that bind to the ADaM site, CBS sites, ATP binding site, and the newly identified C2 binding sites in the γ-subunit via co-crystallization with phosphorylated AMPK (pT172) α2β1γ1 isoform or α2/1β1γ1 chimera. Drugs with binding affinities above 500 nM fail to co-crystallize with AMPK using these parameters. |
Mendeley readers
The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 3 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Professor | 1 | 33% |
Librarian | 1 | 33% |
Unknown | 1 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 1 | 33% |
Earth and Planetary Sciences | 1 | 33% |
Unknown | 1 | 33% |