X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes

Human carbonic anhydrases (CAs) are well studied targets for the development of inhibitors for pharmaceutical applications. The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a —C...

Descripción completa

Detalles Bibliográficos
Autores principales: Fisher, S. Zoë, Govindasamy, Lakshmanan, Boyle, Nicholas, Agbandje-McKenna, Mavis, Silverman, David N., Blackburn, G. Michael, McKenna, Robert
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2006
Materias:
Protein Structure Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242956/
https://www.ncbi.nlm.nih.gov/pubmed/16820676
http://dx.doi.org/10.1107/S1744309106020446

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242956/
https://www.ncbi.nlm.nih.gov/pubmed/16820676
http://dx.doi.org/10.1107/S1744309106020446

Ejemplares similares