5MRK

Structural basis of Zika virus methyltransferase inhibition by sinefungin

Summary for 5MRK

• Entry DOI: 10.2210/pdb5mrk/pdb
• Descriptor: methyltransferase, SINEFUNGIN, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: zika, virus, methyltransferase, sinefungin, transferase
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Cellular location: Virion membrane ; Multi-pass membrane protein : A0A1B0YUR2
• Total number of polymer chains: 2
• Total formula weight: 59456.64

Authors

Hercik, K.,Boura, E. (deposition date: 2016-12-23, release date: 2017-01-25, Last modification date: 2024-10-23)

Primary citation

Hercik, K.,Brynda, J.,Nencka, R.,Boura, E.
Structural basis of Zika virus methyltransferase inhibition by sinefungin.
Arch. Virol., 162:2091-2096, 2017

PubMed Abstract: 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.

PubMed: 28357511
DOI: 10.1007/s00705-017-3345-x

Experimental method

X-RAY DIFFRACTION (1.9 Å)