Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation–π bond

Human liver pyruvate kinase (hLPYK) converts phosphoenolpyruvate to pyruvate in the final step of glycolysis. hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP). The allosteric site, as defined by previous structural studies, is located in domain C between the phosphate-bind...

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Detalhes bibliográficos
Publicado no:Acta Crystallogr F Struct Biol Commun
Main Authors: McFarlane, Jeffrey S., Ronnebaum, Trey A., Meneely, Kathleen M., Chilton, Annemarie, Fenton, Aron W., Lamb, Audrey L.
Formato: Artigo
Idioma:Inglês
Publicado em: International Union of Crystallography 2019
Assuntos:
Research Communications
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC6572093/
https://ncbi.nlm.nih.gov/pubmed/31204694
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X19007209
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