Hugo Heringer de Almeida/5YGH

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==Structure==
==Structure==
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<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> Crystal structure of ZIKV C protein at a resolution of 1.9Å.The structure 5YGH has in total <scene name='Ptroteopedia0001.png '>2 chains</scene>. These are represented by 1 sequence-unique entity. 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. T
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<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> Crystal structure of ZIKV C protein at a resolution of 1.9Å.The structure 5YGH has in total <scene name='78/781908/5ygh_2chain/1'>2 chain</scene>. These are represented by 1 sequence-unique entity. 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. T
== Function ==
== Function ==
Structure of the capsid protein from Zika Virus.
Structure of the capsid protein from Zika Virus.

Revision as of 13:35, 19 March 2018

Contents

Structure

Insert caption here

Drag the structure with the mouse to rotate
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 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. T

Function

Structure of the capsid protein from Zika Virus.

Disease

Zika

Relevance

These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein.

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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