5jxj - Revision history

OCA at 19:14, 20 September 2023

OCA — Wed, 20 Sep 2023 19:14:10 GMT

←Older revision		Revision as of 19:14, 20 September 2023
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	<StructureSection load='5jxj' size='340' side='right'caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5jxj' size='340' side='right'caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jxj]] is a 2 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=5JXJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5JXJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JXJ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~FURIN~~, ~~FUR, PACE, PCSK3 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5jxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxj OCA], [https://pdbe.org/5jxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jxj RCSB], [https://www.ebi.ac.uk/pdbsum/5jxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxj ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Furin Furin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75]~~ </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5jxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxj OCA], [~~http~~://pdbe.org/5jxj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5jxj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5jxj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxj ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN]] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref>	+	[https://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Furin]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arciniega, M]]	+	[[Category: Synthetic construct]]
-	[[Category: Dahms~~, S O~~]]	+	[[Category: Arciniega M]]
-	[[Category: Huber, R]]	+	[[Category: Dahms SO]]
-	[[Category: Steinmetzer, T]]	+	[[Category: Huber R]]
-	[[Category: Than~~, M E]]~~	+	[[Category: Steinmetzer T]]
-	~~[[Category: Hydrolase]]~~	+	[[Category: Than ME]]
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Proteolysis~~]]	+

OCA at 11:44, 17 June 2020

OCA — Wed, 17 Jun 2020 11:44:23 GMT

←Older revision		Revision as of 11:44, 17 June 2020
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	==Structure of the proprotein convertase furin complexed to meta-guanidinomethyl-Phac-RVR-Amba in presence of EDTA==		==Structure of the proprotein convertase furin complexed to meta-guanidinomethyl-Phac-RVR-Amba in presence of EDTA==
-	<StructureSection load='5jxj' size='340' side='right' caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5jxj' size='340' side='right'caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jxj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXJ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JXJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jxj]] is a 2 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=5JXJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JXJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FURIN, FUR, PACE, PCSK3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Furin Furin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Furin Furin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75] </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=5jxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxj OCA], [http://pdbe.org/5jxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxj RCSB], [http://www.ebi.ac.uk/pdbsum/5jxj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxj ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxj OCA], [http://pdbe.org/5jxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxj RCSB], [http://www.ebi.ac.uk/pdbsum/5jxj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5jxj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5jxj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Furin\|Furin]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Furin]]		[[Category: Furin]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arciniega, M]]		[[Category: Arciniega, M]]
	[[Category: Dahms, S O]]		[[Category: Dahms, S O]]

OCA at 09:37, 19 October 2016

OCA — Wed, 19 Oct 2016 09:37:05 GMT

←Older revision		Revision as of 09:37, 19 October 2016
Line 1:		Line 1:

-	==~~Human protease~~ complexed ~~with an inhibitor by soaking~~ in presence of EDTA==	+	==Structure of the proprotein convertase furin complexed to meta-guanidinomethyl-Phac-RVR-Amba in presence of EDTA==
	<StructureSection load='5jxj' size='340' side='right' caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5jxj' size='340' side='right' caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 21:31, 5 October 2016

OCA — Wed, 05 Oct 2016 21:31:42 GMT

←Older revision		Revision as of 21:31, 5 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5jxj is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Human protease complexed with an inhibitor by soaking in presence of EDTA==
		+	<StructureSection load='5jxj' size='340' side='right' caption='[[5jxj]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5jxj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JXJ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Furin Furin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75] </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=5jxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxj OCA], [http://pdbe.org/5jxj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxj RCSB], [http://www.ebi.ac.uk/pdbsum/5jxj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxj ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN]] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Proprotein convertases (PCs) are highly specific proteases required for the proteolytic modification of many secreted proteins. An unbalanced activity of these enzymes is connected to pathologies like cancer, atherosclerosis, hypercholesterolaemia, and infectious diseases. Novel protein crystallographic structures of the prototypical PC family member furin in different functional states were determined to 1.8-2.0 A. These, together with biochemical data and modeling by molecular dynamics calculations, suggest essential elements underlying its unusually high substrate specificity. Furin shows a complex activation mechanism and exists in at least four defined states: (i) the "off state," incompatible with substrate binding as seen in the unliganded enzyme; (ii) the active "on state" seen in inhibitor-bound furin; and the respective (iii) calcium-free and (iv) calcium-bound forms. The transition from the off to the on state is triggered by ligand binding at subsites S1 to S4 and appears to underlie the preferential recognition of the four-residue sequence motif of furin. The molecular dynamics simulations of the four structural states reflect the experimental observations in general and provide approximations of the respective stabilities. Ligation by calcium at the PC-specific binding site II influences the active-site geometry and determines the rotamer state of the oxyanion hole-forming Asn295, and thus adds a second level of the activity modulation of furin. The described crystal forms and the observations of different defined functional states may foster the development of new tools and strategies for pharmacological intervention targeting furin.

-	~~Authors~~:	+	Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.,Dahms SO, Arciniega M, Steinmetzer T, Huber R, Than ME Proc Natl Acad Sci U S A. 2016 Sep 19. pii: 201613630. PMID:27647913<ref>PMID:27647913</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5jxj" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Furin]]
		+	[[Category: Arciniega, M]]
		+	[[Category: Dahms, S O]]
		+	[[Category: Huber, R]]
		+	[[Category: Steinmetzer, T]]
		+	[[Category: Than, M E]]
		+	[[Category: Hydrolase]]
		+	[[Category: Inhibitor]]
		+	[[Category: Protease]]
		+	[[Category: Proteolysis]]

OCA at 13:39, 9 September 2016

OCA — Fri, 09 Sep 2016 13:39:02 GMT

←Older revision		Revision as of 13:39, 9 September 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5jxj is ON HOLD	+	The entry 5jxj is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5jxj" [edit=sysop:move=sysop]

OCA — Wed, 01 Jun 2016 14:00:27 GMT

Protected "5jxj" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:00, 1 June 2016

OCA: New page: '''Unreleased structure''' The entry 5jxj is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 01 Jun 2016 14:00:26 GMT

New page: '''Unreleased structure''' The entry 5jxj is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5jxj is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]