Unknown

Dataset Information

0

X-ray crystallographic structure of a teixobactin analogue reveals key interactions of the teixobactin pharmacophore.


ABSTRACT: The X-ray crystallographic structure of a truncated teixobactin analogue reveals hydrogen-bonding and hydrophobic interactions and a cavity that binds a chloride anion. Minimum inhibitory concentration (MIC) assays against Gram-positive bacteria correlate the observed structure with antibiotic activity.

SUBMITTER: Yang H 

PROVIDER: S-EPMC5381722 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

X-ray crystallographic structure of a teixobactin analogue reveals key interactions of the teixobactin pharmacophore.

Yang H H   Du Bois D R DR   Ziller J W JW   Nowick J S JS  

Chemical communications (Cambridge, England) 20170201 18


The X-ray crystallographic structure of a truncated teixobactin analogue reveals hydrogen-bonding and hydrophobic interactions and a cavity that binds a chloride anion. Minimum inhibitory concentration (MIC) assays against Gram-positive bacteria correlate the observed structure with antibiotic activity. ...[more]

Similar Datasets

| S-EPMC6356018 | biostudies-literature
| S-EPMC5283680 | biostudies-literature
| S-EPMC7814985 | biostudies-literature
| S-EPMC6124899 | biostudies-other
| S-EPMC6677831 | biostudies-literature
| S-EPMC2929266 | biostudies-literature
| S-EPMC6361391 | biostudies-literature
| S-EPMC2203348 | biostudies-literature
| S-EPMC4303302 | biostudies-literature
| S-EPMC1472067 | biostudies-literature