6aez - Revision history

OCA at 09:28, 22 November 2023

OCA — Wed, 22 Nov 2023 09:28:36 GMT

←Older revision		Revision as of 09:28, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='6aez' size='340' side='right'caption='[[6aez]], [[Resolution\|resolution]] 1.63Å' scene=''>		<StructureSection load='6aez' size='340' side='right'caption='[[6aez]], [[Resolution\|resolution]] 1.63Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6aez]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6AEZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6aez]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AEZ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.63Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CCL5, D17S136E, SCYA5 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aez OCA], [~~http~~://pdbe.org/6aez PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6aez RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6aez PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6aez ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aez OCA], [https://pdbe.org/6aez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aez RCSB], [https://www.ebi.ac.uk/pdbsum/6aez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aez ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CCL5_HUMAN CCL5_HUMAN]] Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.<ref>PMID:16791620</ref> <ref>PMID:1380064</ref> <ref>PMID:8525373</ref> <ref>PMID:9516414</ref> <ref>PMID:15923218</ref>	+	[https://www.uniprot.org/uniprot/CCL5_HUMAN CCL5_HUMAN] Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.<ref>PMID:16791620</ref> <ref>PMID:1380064</ref> <ref>PMID:8525373</ref> <ref>PMID:9516414</ref> <ref>PMID:15923218</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~CC-type~~ chemokine ~~ligand 5 (~~CCL5) is ~~involved in the pathogenesis~~ of ~~many~~ inflammatory ~~conditions~~. ~~Under~~ physiological conditions, ~~CCL5 oligomerization~~ and ~~aggregation are~~ considered to be ~~responsible~~ for ~~its inflammatory properties~~. The ~~structural basis~~ of ~~CCL5 oligomerization remains controversial because~~ the ~~current~~ oligomer ~~models contain no consensus interactions. In this study, NMR~~ and ~~biophysical analyses proposed evidence that~~ the ~~CC-type CCL5 dimer acts as the basic unit to constitute~~ the oligomer ~~and that CCL5 oligomerizes alternatively through E66-K25 and E66-R44/K45 interactions~~. ~~In addition~~, a ~~newly determined trimer structure, constituted by~~ CCL5 ~~and the E66S~~ mutant~~, reported an interfacial interaction through the N-terminal~~ (12)~~FAY(14) sequence. The interaction contributes to~~ CCL5 ~~aggregation and precipitation but not~~ to ~~oligomerization~~. ~~In accordance with the observations,~~ an ~~integrative model explains~~ the CCL5 ~~oligomerization and aggregation mechanism in which CCL5 assembly consists of two types of dimer-dimer interactions and one aggregation mechanism. For full-length CCL5~~, the ~~molecular accumulation triggers oligomerization through~~ the ~~E66~~-~~K25 and E66-R44/K45 interactions~~, ~~and~~ the (12)~~FAY~~(14) ~~interaction acts as~~ a ~~secondary effect~~ to ~~derive aggregation~~ and ~~precipitation~~. ~~In contrast,~~ the ~~E66-R44/K45 interaction might dominate~~ in CCL5 ~~N-terminal truncations~~, ~~and the interaction would lead to the filament-like formation~~ in ~~solution~~.	+	The chemokine CCL5 is considered to be a potential therapeutic target because of its ability to recruit immune cells to inflammatory sites. CCL5 aggregates under physiological conditions, and high-order oligomer formation is considered to be significant for cell migration, immune-cell activation and HIV cell entry. The structure of the high-order oligomer is unknown and the mechanism by which the oligomer is derived has yet to be established. Here, a CCL5 mutant (CCL5-E66S) which is deficient in oligomer formation was mixed with native CCL5 to prepare a protein trimer. At an optimized ratio the trimeric CCL5 crystallized, and the crystal belonged to the tetragonal space group P41212, with unit-cell parameters a = 56.6, b = 56.6, c = 154.1 A. The Matthews coefficient (VM) of the crystal is 2.58 A(3) Da(-1) (three molecules in the asymmetric unit), with a solvent content of 52.32%. Diffraction data were collected to a resolution of 1.87 A and the statistics indicated satisfactory data quality. The new structure will reveal the interfaces in the CCL5 oligomer, therefore assisting in understanding the mechanism of CCL5 oligomerization.

-	~~Integrative Model to Coordinate the Oligomerization and Aggregation Mechanisms of~~ CCL5.,Chen YC~~, Chen SP, Li JY, Chen PC, Lee YZ~~, Li KM, Zarivach R, Sun YJ, Sue SC ~~J Mol~~ Biol. ~~2020~~ Feb 14;~~432~~(4):~~1143~~-~~1157~~. doi: 10.~~1016~~/~~j.jmb.2019.12.049~~. Epub~~, 2020~~ Jan 11. PMID:~~31931012~~<ref>PMID:~~31931012~~</ref>	+	Human CCL5 trimer: expression, purification and initial crystallographic studies.,Chen YC, Li KM, Zarivach R, Sun YJ, Sue SC Acta Crystallogr F Struct Biol Commun. 2018 Feb 1;74(Pt 2):82-85. doi:, 10.1107/S2053230X17018544. Epub 2018 Jan 26. PMID:29400316<ref>PMID:29400316</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chen~~, P J~~]]	+	[[Category: Chen PJ]]
-	[[Category: Chen~~, Y C~~]]	+	[[Category: Chen YC]]
-	[[Category: Li~~, K M~~]]	+	[[Category: Li KM]]
-	[[Category: Sue~~, S C~~]]	+	[[Category: Sue SC]]
-	[[Category: Sun~~, Y J~~]]	+	[[Category: Sun YJ]]
-	[[Category: Zarivach, R]]	+	[[Category: Zarivach R]]
-	~~[[Category: Cc-type]]~~	+
-	~~[[Category: Ccl5]]~~	+
-	~~[[Category: Chemokine]]~~	+
-	~~[[Category: Cytokine]]~~	+
-	~~[[Category: Dimer]]~~	+
-	~~[[Category: Oligomer]]~~	+
-	~~[[Category: Rante~~]]	+

OCA at 10:11, 18 March 2020

OCA — Wed, 18 Mar 2020 10:11:23 GMT

←Older revision		Revision as of 10:11, 18 March 2020
Line 12:		Line 12:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~The~~ chemokine CCL5 is ~~considered to be a potential therapeutic target because~~ of ~~its ability to recruit immune cells to~~ inflammatory ~~sites~~. ~~CCL5 aggregates under~~ physiological conditions, and ~~high-order oligomer formation is~~ considered to be ~~significant~~ for ~~cell migration, immune-cell activation and HIV cell entry~~. The ~~structure~~ of the ~~high-order~~ oligomer ~~is unknown~~ and the ~~mechanism by which~~ the oligomer ~~is derived has yet to be established~~. ~~Here~~, a CCL5 mutant (~~CCL5-E66S~~) ~~which is deficient in oligomer formation was mixed with native~~ CCL5 to ~~prepare a protein trimer~~. At an ~~optimized ratio~~ the ~~trimeric~~ CCL5 ~~crystallized~~, ~~and~~ the ~~crystal belonged to~~ the ~~tetragonal space group P41212, with unit~~-~~cell parameters a = 56.6~~, ~~b = 56.6, c = 154.1 A. The Matthews coefficient (VM) of~~ the ~~crystal is 2.58 A~~(3) Da(-1) ~~(three molecules in the asymmetric unit), with~~ a ~~solvent content of 52.32%. Diffraction data were collected~~ to ~~a resolution of 1.87 A~~ and ~~the statistics indicated satisfactory data quality~~. ~~The new structure will reveal~~ the ~~interfaces~~ in ~~the~~ CCL5 ~~oligomer~~, ~~therefore assisting~~ in ~~understanding the mechanism of CCL5 oligomerization~~.	+	CC-type chemokine ligand 5 (CCL5) is involved in the pathogenesis of many inflammatory conditions. Under physiological conditions, CCL5 oligomerization and aggregation are considered to be responsible for its inflammatory properties. The structural basis of CCL5 oligomerization remains controversial because the current oligomer models contain no consensus interactions. In this study, NMR and biophysical analyses proposed evidence that the CC-type CCL5 dimer acts as the basic unit to constitute the oligomer and that CCL5 oligomerizes alternatively through E66-K25 and E66-R44/K45 interactions. In addition, a newly determined trimer structure, constituted by CCL5 and the E66S mutant, reported an interfacial interaction through the N-terminal (12)FAY(14) sequence. The interaction contributes to CCL5 aggregation and precipitation but not to oligomerization. In accordance with the observations, an integrative model explains the CCL5 oligomerization and aggregation mechanism in which CCL5 assembly consists of two types of dimer-dimer interactions and one aggregation mechanism. For full-length CCL5, the molecular accumulation triggers oligomerization through the E66-K25 and E66-R44/K45 interactions, and the (12)FAY(14) interaction acts as a secondary effect to derive aggregation and precipitation. In contrast, the E66-R44/K45 interaction might dominate in CCL5 N-terminal truncations, and the interaction would lead to the filament-like formation in solution.

-	~~Human~~ CCL5 ~~trimer: expression, purification and initial crystallographic studies~~.,Chen YC, Li KM, Zarivach R, Sun YJ, Sue SC ~~Acta Crystallogr F Struct~~ Biol ~~Commun~~. ~~2018~~ Feb 1;74(~~Pt 2~~):82-85. doi:, 10.~~1107~~/~~S2053230X17018544~~. Epub ~~2018~~ Jan 26. PMID:~~29400316~~<ref>PMID:~~29400316~~</ref>	+	Integrative Model to Coordinate the Oligomerization and Aggregation Mechanisms of CCL5.,Chen YC, Chen SP, Li JY, Chen PC, Lee YZ, Li KM, Zarivach R, Sun YJ, Sue SC J Mol Biol. 2020 Feb 14;432(4):1143-1157. doi: 10.1016/j.jmb.2019.12.049. Epub, 2020 Jan 11. PMID:31931012<ref>PMID:31931012</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

OCA at 09:15, 18 December 2019

OCA — Wed, 18 Dec 2019 09:15:34 GMT

←Older revision		Revision as of 09:15, 18 December 2019
Line 3:		Line 3:
	<StructureSection load='6aez' size='340' side='right'caption='[[6aez]], [[Resolution\|resolution]] 1.63Å' scene=''>		<StructureSection load='6aez' size='340' side='right'caption='[[6aez]], [[Resolution\|resolution]] 1.63Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6aez]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6aez]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CCL5, D17S136E, SCYA5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aez OCA], [http://pdbe.org/6aez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aez RCSB], [http://www.ebi.ac.uk/pdbsum/6aez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aez ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aez OCA], [http://pdbe.org/6aez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aez RCSB], [http://www.ebi.ac.uk/pdbsum/6aez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aez ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CCL5_HUMAN CCL5_HUMAN]] Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.<ref>PMID:16791620</ref> <ref>PMID:1380064</ref> <ref>PMID:8525373</ref> <ref>PMID:9516414</ref> <ref>PMID:15923218</ref>		[[http://www.uniprot.org/uniprot/CCL5_HUMAN CCL5_HUMAN]] Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.<ref>PMID:16791620</ref> <ref>PMID:1380064</ref> <ref>PMID:8525373</ref> <ref>PMID:9516414</ref> <ref>PMID:15923218</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The chemokine CCL5 is considered to be a potential therapeutic target because of its ability to recruit immune cells to inflammatory sites. CCL5 aggregates under physiological conditions, and high-order oligomer formation is considered to be significant for cell migration, immune-cell activation and HIV cell entry. The structure of the high-order oligomer is unknown and the mechanism by which the oligomer is derived has yet to be established. Here, a CCL5 mutant (CCL5-E66S) which is deficient in oligomer formation was mixed with native CCL5 to prepare a protein trimer. At an optimized ratio the trimeric CCL5 crystallized, and the crystal belonged to the tetragonal space group P41212, with unit-cell parameters a = 56.6, b = 56.6, c = 154.1 A. The Matthews coefficient (VM) of the crystal is 2.58 A(3) Da(-1) (three molecules in the asymmetric unit), with a solvent content of 52.32%. Diffraction data were collected to a resolution of 1.87 A and the statistics indicated satisfactory data quality. The new structure will reveal the interfaces in the CCL5 oligomer, therefore assisting in understanding the mechanism of CCL5 oligomerization.
		+
		+	Human CCL5 trimer: expression, purification and initial crystallographic studies.,Chen YC, Li KM, Zarivach R, Sun YJ, Sue SC Acta Crystallogr F Struct Biol Commun. 2018 Feb 1;74(Pt 2):82-85. doi:, 10.1107/S2053230X17018544. Epub 2018 Jan 26. PMID:29400316<ref>PMID:29400316</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6aez" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Chen, P J]]		[[Category: Chen, P J]]

OCA at 05:46, 7 August 2019

OCA — Wed, 07 Aug 2019 05:46:01 GMT

←Older revision		Revision as of 05:46, 7 August 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6aez is ~~ON HOLD until Aug 07 2020~~	+	==Crystal structure of human CCL5 trimer==
-		+	<StructureSection load='6aez' size='340' side='right'caption='[[6aez]], [[Resolution\|resolution]] 1.63Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6aez]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEZ FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aez OCA], [http://pdbe.org/6aez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aez RCSB], [http://www.ebi.ac.uk/pdbsum/6aez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aez ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CCL5_HUMAN CCL5_HUMAN]] Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.<ref>PMID:16791620</ref> <ref>PMID:1380064</ref> <ref>PMID:8525373</ref> <ref>PMID:9516414</ref> <ref>PMID:15923218</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Chen, P J]]
		+	[[Category: Chen, Y C]]
		+	[[Category: Li, K M]]
		+	[[Category: Sue, S C]]
		+	[[Category: Sun, Y J]]
		+	[[Category: Zarivach, R]]
		+	[[Category: Cc-type]]
		+	[[Category: Ccl5]]
		+	[[Category: Chemokine]]
		+	[[Category: Cytokine]]
		+	[[Category: Dimer]]
		+	[[Category: Oligomer]]
		+	[[Category: Rante]]

OCA at 04:05, 24 October 2018

OCA — Wed, 24 Oct 2018 04:05:45 GMT

←Older revision		Revision as of 04:05, 24 October 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6aez is ON HOLD	+	The entry 6aez is ON HOLD until Aug 07 2020

	Authors:		Authors:

OCA: Protected "6aez" [edit=sysop:move=sysop]

OCA — Wed, 15 Aug 2018 14:39:20 GMT

Protected "6aez" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:39, 15 August 2018

OCA: New page: '''Unreleased structure''' The entry 6aez is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 15 Aug 2018 14:39:19 GMT

New page: '''Unreleased structure''' The entry 6aez is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6aez is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]