Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase
N-Myristoyltransferase (NMT) has been shown to be an attractive target for the development of novel therapeutic agents for the treatment of human African trypanosomiasis. A fragment library has been screened using NMR spectroscopy and the binding mode of the hits was confirmed by X-ray crystallogra...
Main Authors: | , |
---|---|
Format: | Online |
Language: | English |
Published: |
International Union of Crystallography
2015
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427169/ |
id |
pubmed-4427169 |
---|---|
recordtype |
oai_dc |
spelling |
pubmed-44271692015-05-25 Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase Robinson, David A. Wyatt, Paul G. Molecular Parasitology N-Myristoyltransferase (NMT) has been shown to be an attractive target for the development of novel therapeutic agents for the treatment of human African trypanosomiasis. A fragment library has been screened using NMR spectroscopy and the binding mode of the hits was confirmed by X-ray crystallography using L. major NMT as a structural surrogate. International Union of Crystallography 2015-04-21 /pmc/articles/PMC4427169/ /pubmed/25945713 http://dx.doi.org/10.1107/S2053230X15003040 Text en © Robinson & Wyatt 2015 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Robinson, David A. Wyatt, Paul G. |
spellingShingle |
Robinson, David A. Wyatt, Paul G. Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
author_facet |
Robinson, David A. Wyatt, Paul G. |
author_sort |
Robinson, David A. |
title |
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
title_short |
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
title_full |
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
title_fullStr |
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
title_full_unstemmed |
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase |
title_sort |
identification and structure solution of fragment hits against kinetoplastid n-myristoyltransferase |
description |
N-Myristoyltransferase (NMT) has been shown to be an attractive target for the development of novel therapeutic agents for the treatment of human African trypanosomiasis. A fragment library has been screened using NMR spectroscopy and the binding mode of the hits was confirmed by X-ray crystallography using L. major NMT as a structural surrogate. |
publisher |
International Union of Crystallography |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427169/ |
_version_ |
1613221788307685376 |