5ulp | pdb_00005ulp
From Proteopedia
Structure of the NS5 methyltransferase from Zika bound to MS2042
| ||||||||||||
Structural highlights
Publication Abstract from PubMedThe Zika virus (ZIKV) has emerged as a major health hazard. We present here a high resolution structure (1.55 A) of ZIKV NS5 methyltransferase bound to a novel S-adenosylmethionine (SAM) analog in which a 4-fluorophenyl moiety substitutes for the methyl group. We show that the 4-fluorophenyl moiety extends into a portion of the RNA binding tunnel that typically contains the adenosine 2'OH of the RNA-cap moiety. Together, the new SAM analog and the high-resolution crystal structure are a step towards the development of antivirals against ZIKV and other flaviviruses. Development of a S-adenosylmethionine analog that intrudes the RNA-cap binding site of Zika methyltransferase.,Jain R, Butler KV, Coloma J, Jin J, Aggarwal AK Sci Rep. 2017 May 9;7(1):1632. doi: 10.1038/s41598-017-01756-7. PMID:28487506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 10:03, 3 August 2017.