Structural basis of Zika virus methyltransferase inhibition by sinefungin

Zika virus is considered a major global threat to human kind. Here, we present a crystal structure of one of its essential enzymes, the methyltransferase, with the inhibitor sinefungin. This structure, together with previously solved structures with bound substrates, will provide the information nee...

Full description

Saved in:
Bibliographic Details
Published in:Archives of virology 2017-07, Vol.162 (7), p.2091-2096
Main Authors: Hercik, Kamil, Brynda, Jiri, Nencka, Radim, Boura, Evzen
Format: Article
Language:English
Subjects:
Adenine
Adenosine - analogs & derivatives
Adenosine - chemistry
Binding Sites
Biomedical and Life Sciences
Biomedicine
Brief Report
Crystal structure
Enzyme Inhibitors - chemistry
Enzymes
Guanosine triphosphate
Infectious Diseases
Medical Microbiology
Methyltransferase
Methyltransferases - antagonists & inhibitors
Models, Molecular
Protein Binding
Virology
Zika virus
Zika Virus - enzymology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Zika virus is considered a major global threat to human kind. Here, we present a crystal structure of one of its essential enzymes, the methyltransferase, with the inhibitor sinefungin. This structure, together with previously solved structures with bound substrates, will provide the information needed for rational inhibitor design. Based on the structural data we suggest the modification of the adenine moiety of sinefungin to increase selectivity and to covalently link it to a GTP analogue, to increase the affinity of the synthesized compounds.
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-017-3345-x