B Zhao

C Kobayashi

D Hamelberg

J-P Ryckaert

JM Johnston

K Kappel

L Mlera

LCT Pierce

M Kapoor

O Faye

PM Gasper

PRL Markwick

R Al-Hasani

T Darden

T Shen

TJ Chambers

Y Miao

Y Wang

AbstractSince 2015, widespread Zika virus outbreaks in Central and South America have caused increases in microcephaly cases, and this acute problem requires urgent attention. We employed molecular dynamics and Gaussian accelerated molecular dynamics techniques to investigate the structure of Zika NS5 protein with S-adenosyl-L-homocysteine (SAH) and an RNA analogue, namely 7-methylguanosine 5′-triphosphate (m7GTP). For the binding motif of Zika virus NS5 protein and SAH, we suggest that the four Zika NS5 substructures (residue orders: 101–112, 54–86, 127–136 and 146–161) and the residues (Ser56, Gly81, Arg84, Trp87, Thr104, Gly106, Gly107, His110, Asp146, Ile147, and Gly148) might be responsible for the selectivity of the new Zika virus drugs. For the binding motif of Zika NS5 protein and m7GTP, we suggest that the three Zika NS5 substructures (residue orders: 11–31, 146–161 and 207–218) and the residues (Asn17, Phe24, Lys28, Lys29, Ser150, Arg213, and Ser215) might be responsible for the selectivity of the new Zika virus drugs.</jats:p

Chih-Hung Chuang

Shean-jaw Chiou

Tian-Lu Cheng

Yeng-Tseng Wang

Crossref

Scientific Reports

A molecular dynamics simulation study decodes the Zika virus NS5 methyltransferase bound to SAH and RNA analogue

A molecular dynamics simulation study decodes the Zika virus NS5 methyltransferase bound to SAH and RNA analogue

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