Roza Kalabekova, Caitlin M. Quinn, Kumar Tekwani Movellan, Angela M. Gronenborn*, Mikael Akke* and Tatyana Polenova*,
{"title":"19F 快速魔角旋转核磁共振波谱分析含氟配体与 Galectin-3 碳水化合物识别域的微晶复合物","authors":"Roza Kalabekova, Caitlin M. Quinn, Kumar Tekwani Movellan, Angela M. Gronenborn*, Mikael Akke* and Tatyana Polenova*, ","doi":"10.1021/acs.biochem.4c0023210.1021/acs.biochem.4c00232","DOIUrl":null,"url":null,"abstract":"<p >Structural characterization of protein–ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast <sup>19</sup>F- and <sup>1</sup>H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D <sup>13</sup>C–<sup>19</sup>F and <sup>1</sup>H–<sup>19</sup>F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that <sup>19</sup>F MAS NMR is a powerful tool for detailed characterization of protein–ligand interfaces and protein interactions at the atomic level.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":null,"pages":null},"PeriodicalIF":2.9000,"publicationDate":"2024-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"19F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3\",\"authors\":\"Roza Kalabekova, Caitlin M. Quinn, Kumar Tekwani Movellan, Angela M. Gronenborn*, Mikael Akke* and Tatyana Polenova*, \",\"doi\":\"10.1021/acs.biochem.4c0023210.1021/acs.biochem.4c00232\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Structural characterization of protein–ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast <sup>19</sup>F- and <sup>1</sup>H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D <sup>13</sup>C–<sup>19</sup>F and <sup>1</sup>H–<sup>19</sup>F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that <sup>19</sup>F MAS NMR is a powerful tool for detailed characterization of protein–ligand interfaces and protein interactions at the atomic level.</p>\",\"PeriodicalId\":28,\"journal\":{\"name\":\"Biochemistry Biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.9000,\"publicationDate\":\"2024-07-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry Biochemistry\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.biochem.4c00232\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry Biochemistry","FirstCategoryId":"1","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.biochem.4c00232","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
19F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3
Structural characterization of protein–ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast 19F- and 1H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D 13C–19F and 1H–19F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that 19F MAS NMR is a powerful tool for detailed characterization of protein–ligand interfaces and protein interactions at the atomic level.
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