Hugo Heringer de Almeida/5YGH

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	== 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.
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	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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Revision as of 12:52, 5 March 2018

Contents 1 Structure 2 Function 3 Disease 4 Relevance 5 Structural highlights 6 References 7 OBS.:

Structure

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

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 discipline in University of São Paulo