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Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition

Abstract:
Crystallographic analyses of the VIM-5 metallo-β-lactamase (MBL) with isoquinoline inhibitors reveal non zinc ion binding modes. Comparison with other MBL-inhibitor structures directed addition of a zinc-binding thiol enabling identification of potent B1 MBL inhibitors. The inhibitors potentiate meropenem activity against clinical isolates harboring MBLs.
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1039/c7cc02394d

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Institution:
University of Oxford
Department:
Chemistry; Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
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Funding agency for:
Schofield, CJ
Wellcome Trust More from this funder
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
53
Issue:
43
Pages:
5806-5809
Publication date:
2017-04-25
Acceptance date:
2017-04-25
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:692202
URN:
uri:299072f3-9b26-4398-8673-243a4336b9d7
UUID:
uuid:299072f3-9b26-4398-8673-243a4336b9d7
Local pid:
pubs:692202
Paper number:
43
Language:
English

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