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Hugo Heringer de Almeida/5YGH

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==OBS.:==
==OBS.:==
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This article is a small test for a discipline in University of São Paulo
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This article is a small test for a biochemistry class in University of São Paulo

Revision as of 16:40, 8 March 2018

Contents

Structure

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Crystal structure of ZIKV C protein at a resolution of 1.9Å. The ZIKV C protein structure contains four α helices with a long pre-α1 loop 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. These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein.

Function

Structure of the capsid protein from Zika Virus.

Disease

Zika

Relevance

The capsid protein can be recognise by Lymphocytes.

Structural highlights

The structure 5YGH has in total 2 chains. These are represented by 1 sequence-unique entity.

References

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.:

This article is a small test for a biochemistry class in University of São Paulo

Proteopedia Page Contributors and Editors (what is this?)

Hugo Heringer de Almeida, Luis Netto, Michal Harel

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