Hugo Heringer de Almeida/5YGH
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Crystal structure of ZIKV C protein at a resolution of 1.9Å.?The structure 5YGH has in total . These are represented by 1 sequence-unique entity. The ZIKV C protein structure contains with a long and forms dimers. The unique long pre-α1 loop in ZIKV C contributes to the tighter association of dimeric assembly and renders a divergent hydrophobic feature at the lipid bilayer interface in comparison with the known C structures of West Nile and dengue viruses. We reported the interaction between the ZIKV C protein and lipid droplets through confocal microscopy analysis. Substitutions of key amino acids in the pre-α1 loop of ZIKV C disrupted the interaction with lipid droplets, indicating that the loop is critical for membrane association. We also recognized that ZIKV C protein possesses broad binding capability to different nucleotide types, including single-stranded and double-stranded RNAs or DNAs. Furthermore, the highly positively charged interface, mainly formed by α4 helix, is proposed to be responsible for nucleotide binding.
FunctionFunction
Structure of the capsid protein from Zika Virus.
DiseaseDisease
Zika
RelevanceRelevance
These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein.
ReferencesReferences
Shang Z., Song H., Shi Y., Qi J., Gao GF. Crystal Structure of the Capsid Protein from Zika Virus. DOI: 10.1016/j.jmb.2018.02.006
OBS.:OBS.:
This article is a small test for a biochemistry class in University of São Paulo