Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases
River blindness, a disease affecting millions throughout the tropics, is caused by parasitic worms. Here, Yuet al. report the discovery and structural characterization of potent macrocyclic peptide inhibitors of iPGM, a nematode-specific phosphoglycerate mutase, as potential leads for novel antimicr...
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2017-04-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms14932 |
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doaj-39345025d3334fe096b7ce4373349fee |
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Article |
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doaj-39345025d3334fe096b7ce4373349fee2021-05-11T07:07:51ZengNature Publishing GroupNature Communications2041-17232017-04-018111310.1038/ncomms14932Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutasesHao Yu0Patricia Dranchak1Zhiru Li2Ryan MacArthur3Matthew S. Munson4Nurjahan Mehzabeen5Nathan J. Baird6Kevin P. Battalie7David Ross8Scott Lovell9Clotilde K. S. Carlow10Hiroaki Suga11James Inglese12Department of Chemistry, Graduate School of Sciences, The University of TokyoNational Center for Advancing Translational Sciences, National Institutes of HealthDivision of Genome Biology, New England BiolabsNational Center for Advancing Translational Sciences, National Institutes of HealthNational Institute of Standards and TechnologyProton Structure Laboratory, Structural Biology Center, University of KansasNational Heart, Lung and Blood Institute, National Institutes of HealthIMCA-CAT Advanced Photon Source, Argonne National LaboratoryNational Institute of Standards and TechnologyProton Structure Laboratory, Structural Biology Center, University of KansasDivision of Genome Biology, New England BiolabsDepartment of Chemistry, Graduate School of Sciences, The University of TokyoNational Center for Advancing Translational Sciences, National Institutes of HealthRiver blindness, a disease affecting millions throughout the tropics, is caused by parasitic worms. Here, Yuet al. report the discovery and structural characterization of potent macrocyclic peptide inhibitors of iPGM, a nematode-specific phosphoglycerate mutase, as potential leads for novel antimicrobial agents.https://doi.org/10.1038/ncomms14932 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Hao Yu Patricia Dranchak Zhiru Li Ryan MacArthur Matthew S. Munson Nurjahan Mehzabeen Nathan J. Baird Kevin P. Battalie David Ross Scott Lovell Clotilde K. S. Carlow Hiroaki Suga James Inglese |
| spellingShingle |
Hao Yu Patricia Dranchak Zhiru Li Ryan MacArthur Matthew S. Munson Nurjahan Mehzabeen Nathan J. Baird Kevin P. Battalie David Ross Scott Lovell Clotilde K. S. Carlow Hiroaki Suga James Inglese Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases Nature Communications |
| author_facet |
Hao Yu Patricia Dranchak Zhiru Li Ryan MacArthur Matthew S. Munson Nurjahan Mehzabeen Nathan J. Baird Kevin P. Battalie David Ross Scott Lovell Clotilde K. S. Carlow Hiroaki Suga James Inglese |
| author_sort |
Hao Yu |
| title |
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| title_short |
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| title_full |
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| title_fullStr |
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| title_full_unstemmed |
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| title_sort |
macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2017-04-01 |
| description |
River blindness, a disease affecting millions throughout the tropics, is caused by parasitic worms. Here, Yuet al. report the discovery and structural characterization of potent macrocyclic peptide inhibitors of iPGM, a nematode-specific phosphoglycerate mutase, as potential leads for novel antimicrobial agents. |
| url |
https://doi.org/10.1038/ncomms14932 |
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