Hugo Heringer de Almeida/5YGH
From Proteopedia
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==Structure== | ==Structure== | ||
| - | <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 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. | + | <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 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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== Function == | == Function == | ||
Structure of the capsid protein from Zika Virus. | Structure of the capsid protein from Zika Virus. | ||
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Zika | Zika | ||
== Relevance == | == Relevance == | ||
| - | + | These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein. | |
== Structural highlights == | == Structural highlights == | ||
The structure 5YGH has in total 2 chains. These are represented by 1 sequence-unique entity. | The structure 5YGH has in total 2 chains. These are represented by 1 sequence-unique entity. | ||
Revision as of 16:44, 8 March 2018
Contents |
Structure
|
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.
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
