Crystallization (Comment) | Organism |
---|---|
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
soraphen A | macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase | Homo sapiens |
Organism | UniProt | Comment | Textmining |
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Homo sapiens | O00763 | - |
- |