Hugo Heringer de Almeida/5YGH - Revision history

Michal Harel at 09:27, 20 January 2019

Michal Harel — Sun, 20 Jan 2019 09:27:55 GMT

←Older revision		Revision as of 09:27, 20 January 2019
Line 1:		Line 1:
-	<Structure load='5YGH' size='350' frame='true' align='right' caption='~~Insert caption here~~' 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.	+	<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.
-		+
-	~~test test~~	+

	== Function ==		== Function ==

Luis Netto at 19:58, 12 April 2018

Luis Netto — Thu, 12 Apr 2018 19:58:03 GMT

←Older revision		Revision as of 19:58, 12 April 2018
Line 1:		Line 1:
	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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.		<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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.
		+
		+	test test

	== Function ==		== Function ==

Hugo Heringer de Almeida at 14:12, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 14:12:05 GMT

←Older revision		Revision as of 14:12, 19 March 2018
Line 1:		Line 1:
-		+	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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.
-	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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 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.	+

	== Function ==		== Function ==

Hugo Heringer de Almeida at 14:08, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 14:08:32 GMT

←Older revision		Revision as of 14:08, 19 March 2018
Line 1:		Line 1:

		+	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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 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='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 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.

Hugo Heringer de Almeida at 14:05, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 14:05:39 GMT

←Older revision		Revision as of 14:05, 19 March 2018
Line 1:		Line 1:

-	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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 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	+
		+	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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 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.

Hugo Heringer de Almeida at 13:40, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 13:40:37 GMT

←Older revision		Revision as of 13:40, 19 March 2018
Line 1:		Line 1:
-	~~==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 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	+	<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' 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 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.

Hugo Heringer de Almeida at 13:35, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 13:35:49 GMT

←Older revision		Revision as of 13:35, 19 March 2018
Line 1:		Line 1:
	==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 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	+	<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.

Hugo Heringer de Almeida at 13:12, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 13:12:28 GMT

←Older revision		Revision as of 13:12, 19 March 2018
Line 1:		Line 1:
	==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 structure 5YGH has in total <scene name='~~Image:Sele~~.~~pdb~~'>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	+	<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
	== Function ==		== Function ==
	Structure of the capsid protein from Zika Virus.		Structure of the capsid protein from Zika Virus.

Hugo Heringer de Almeida at 13:06, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 13:06:13 GMT

←Older revision		Revision as of 13:06, 19 March 2018
Line 1:		Line 1:
	==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 structure 5YGH has in total <scene name='~~Hemoglobin/Foursubunits/5~~'>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	+	<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='Image:Sele.pdb'>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
	== Function ==		== Function ==
	Structure of the capsid protein from Zika Virus.		Structure of the capsid protein from Zika Virus.

Hugo Heringer de Almeida at 13:04, 19 March 2018

Hugo Heringer de Almeida — Mon, 19 Mar 2018 13:04:35 GMT

←Older revision		Revision as of 13:04, 19 March 2018
Line 1:		Line 1:
	==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. T	+	<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='Hemoglobin/Foursubunits/5'>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
	== Function ==		== Function ==
	Structure of the capsid protein from Zika Virus.		Structure of the capsid protein from Zika Virus.
Line 7:		Line 7:
	== Relevance ==		== Relevance ==
	These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein.		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 ==		== 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		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.:==		==OBS.:==
	This article is a small test for a biochemistry class in University of São Paulo		This article is a small test for a biochemistry class in University of São Paulo