Hugo Heringer de Almeida/5YGH

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Revision as of 11:52, 5 March 2018 (edit) Hugo Heringer de Almeida (Talk | contribs) ← Previous diff		Current revision (09:27, 20 January 2019) (edit) (undo) Michal Harel (Talk | contribs)
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-	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />==Your Heading Here (maybe something like 'The structure 5YGH has in total 2 chains. These are represented by 1 sequence-unique entity.')==	+	<Structure load='5YGH' size='350' frame='true' align='right' caption='Zika virus capsid protein (PDB code [[5ygh]])' scene='78/781908/Surface_5ygh/1' /> 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 <scene name='78/781908/All_loop/1'> four α helices</scene> with a long <scene name='78/781908/Pre_a1_loop/1'>pre-α1 loop</scene> 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.
-	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>	+
-	This is a default text for your page '''Hugo Heringer de Almeida/5YGH'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.	+
-	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.	+
	== Function ==		== Function ==
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	Zika		Zika
	== Relevance ==		== Relevance ==
-	The capsid protein can be recognise by Lymphocytes.	+	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.	+
-	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.	+
-		+
-	</StructureSection>	+
	== References ==		== References ==
-	<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

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Current revision

spinqualitylabelsall models Zika virus capsid protein (PDB code 5ygh) 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 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.

Contents 1 Function 2 Disease 3 Relevance 4 References 5 OBS.:

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