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...

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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
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author Fisher, S. Zoë
Govindasamy, Lakshmanan
Boyle, Nicholas
Agbandje-McKenna, Mavis
Silverman, David N.
Blackburn, G. Michael
McKenna, Robert
author_facet Fisher, S. Zoë
Govindasamy, Lakshmanan
Boyle, Nicholas
Agbandje-McKenna, Mavis
Silverman, David N.
Blackburn, G. Michael
McKenna, Robert
author_sort Fisher, S. Zoë
collection PubMed
description 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 —CF(2)— or —­CHNH(2)— spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs.
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spelling pubmed-22429562008-03-13 X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes Fisher, S. Zoë Govindasamy, Lakshmanan Boyle, Nicholas Agbandje-McKenna, Mavis Silverman, David N. Blackburn, G. Michael McKenna, Robert Acta Crystallogr Sect F Struct Biol Cryst Commun Protein Structure Communications 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 —CF(2)— or —­CHNH(2)— spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs. International Union of Crystallography 2006-06-10 /pmc/articles/PMC2242956/ /pubmed/16820676 http://dx.doi.org/10.1107/S1744309106020446 Text en © International Union of Crystallography 2006 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.
spellingShingle Protein Structure Communications
Fisher, S. Zoë
Govindasamy, Lakshmanan
Boyle, Nicholas
Agbandje-McKenna, Mavis
Silverman, David N.
Blackburn, G. Michael
McKenna, Robert
X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title_full X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title_fullStr X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title_full_unstemmed X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title_short X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
title_sort x-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes
topic Protein Structure Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242956/
https://www.ncbi.nlm.nih.gov/pubmed/16820676
http://dx.doi.org/10.1107/S1744309106020446
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