An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme

BACKGROUND: The structure, function and reaction mechanism of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) have been extensively studied. Based on these studies, three anion binding sites have been identified, one 'Ps' site (for binding the C-3 phosphate of the substrate) and two sites...

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Detalles Bibliográficos
Autores principales: Cook, William J, Senkovich, Olga, Chattopadhyay, Debasish
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2662861/
https://www.ncbi.nlm.nih.gov/pubmed/19243605
http://dx.doi.org/10.1186/1472-6807-9-9

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2662861/
https://www.ncbi.nlm.nih.gov/pubmed/19243605
http://dx.doi.org/10.1186/1472-6807-9-9

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