Journal article
High-throughput crystallography reveals boron-containing inhibitors of a penicillin-binding protein with di- and tricovalent binding modes
- Abstract:
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The effectiveness of β-lactam antibiotics is increasingly compromised by β-lactamases. Boron-containing inhibitors are potent serine-β-lactamase inhibitors, but the interactions of boron-based compounds with the penicillin-binding protein (PBP) β-lactam targets have not been extensively studied. We used high-throughput X-ray crystallography to explore reactions of a boron-containing fragment set with the Pseudomonas aeruginosa PBP3 (PaPBP3). Multiple crystal structures reveal that boronic aci...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, 7.8MB)
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- Publisher copy:
- 10.1021/acs.jmedchem.1c00717
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Authors
Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Journal of Medicinal Chemistry Journal website
- Volume:
- 64
- Issue:
- 15
- Pages:
- 11379-11394
- Place of publication:
- United States
- Publication date:
- 2021-07-31
- Acceptance date:
- 2020-10-30
- DOI:
- EISSN:
-
1520-4804
- ISSN:
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0022-2623
- Pmid:
-
34337941
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
1189500
- Local pid:
- pubs:1189500
- Deposit date:
- 2021-09-17
Terms of use
- Copyright holder:
- Newman et al.
- Copyright date:
- 2021
- Rights statement:
- ©2021 The Authors. Published by American Chemical Society. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).
- Licence:
- CC Attribution (CC BY)
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