6eqv - Revision history

OCA at 10:21, 15 November 2023

OCA — Wed, 15 Nov 2023 10:21:54 GMT

←Older revision		Revision as of 10:21, 15 November 2023
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	<StructureSection load='6eqv' size='340' side='right'caption='[[6eqv]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6eqv' size='340' side='right'caption='[[6eqv]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6eqv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6EQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6eqv]] 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=6EQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EQV 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]] 1.895Å</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=~~CIR~~:~~CITRULLINE~~'>~~CIR~~</scene>, <scene name='pdbligand=~~HY1~~:~~PHENYLACETALDEHYDE~~'>~~HY1~~</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIR:CITRULLINE'>CIR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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'>[https://proteopedia.org/fgij/fg.htm?mol=6eqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqv OCA], [https://pdbe.org/6eqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eqv RCSB], [https://www.ebi.ac.uk/pdbsum/6eqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqv 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=6eqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqv OCA], [~~http~~://pdbe.org/6eqv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6eqv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6eqv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqv 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: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Dahms, S O~~]]	+	[[Category: Synthetic construct]]
-	[[Category: ~~Than, M E~~]]	+	[[Category: Dahms SO]]
-	[[Category: ~~Citrullin]]~~	+	[[Category: Than ME]]
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Proprotein convertase]]~~	+
-	~~[[Category: Protease~~]]	+

OCA at 09:14, 11 November 2020

OCA — Wed, 11 Nov 2020 09:14:00 GMT

←Older revision		Revision as of 09:14, 11 November 2020
Line 1:		Line 1:

	==X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba==		==X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba==
-	<StructureSection load='6eqv' size='340' side='right' caption='[[6eqv]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='6eqv' size='340' side='right'caption='[[6eqv]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6eqv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQV OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6EQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6eqv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EQV 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=CIR:CITRULLINE'>CIR</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</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=CIR:CITRULLINE'>CIR</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</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='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=6eqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqv OCA], [http://pdbe.org/6eqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqv RCSB], [http://www.ebi.ac.uk/pdbsum/6eqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqv 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=6eqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqv OCA], [http://pdbe.org/6eqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqv RCSB], [http://www.ebi.ac.uk/pdbsum/6eqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 6eqv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6eqv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Furin\|Furin]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Furin]]		[[Category: Furin]]
		+	[[Category: Large Structures]]
	[[Category: Dahms, S O]]		[[Category: Dahms, S O]]
	[[Category: Than, M E]]		[[Category: Than, M E]]

OCA at 06:37, 28 February 2018

OCA — Wed, 28 Feb 2018 06:37:43 GMT

←Older revision		Revision as of 06:37, 28 February 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6eqv is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba==
		+	<StructureSection load='6eqv' size='340' side='right' caption='[[6eqv]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6eqv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EQV 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=CIR:CITRULLINE'>CIR</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</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=6eqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqv OCA], [http://pdbe.org/6eqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqv RCSB], [http://www.ebi.ac.uk/pdbsum/6eqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqv 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 ==
		+	The proprotein convertase furin is a highly specific serine protease modifying and thereby activating proteins in the secretory pathway by proteolytic cleavage. Its substrates are involved in many diseases, including cancer and infections caused by bacteria and viruses. Understanding furin's substrate specificity is crucially important for the development of pharmacologically applicable inhibitors. Using protein X-ray crystallography, we investigated the extended substrate binding site of furin in complex with three peptide-derived inhibitors at up to 1.9 A resolution. The structure of the protease bound with a hexapeptide inhibitor revealed molecular details of its S6 pocket, which remained completely unknown so far. The arginine residue at P6 induced an unexpected turnlike conformation of the inhibitor backbone, which is stabilized by intra- and intermolecular H-bonds. In addition, we confirmed the binding of arginine to the previously proposed S5 pocket (S51). An alternative S5 site (S52) could be utilized by shorter side chains as demonstrated for a 4-aminomethyl-phenylacetyl residue, which shows steric properties similar to those of a lysine side chain. Interestingly, we also observed binding of a peptide with citrulline at P4 substituting for the highly conserved arginine. The structural data might indicate an unusual protonation state of Asp264 maintaining the interaction with uncharged citrulline. The herein identified molecular interaction sites at P5 and P6 can be utilized to improve next-generation furin inhibitors. Our data will also help to predict furin substrates more precisely on the basis of the additional specificity determinants observed for P5 and P6.

-	~~Authors:~~ Dahms, ~~S.O.~~, ~~Than~~, M.E.	+	X-ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants beyond the S4 Pocket.,Dahms SO, Hardes K, Steinmetzer T, Than ME Biochemistry. 2018 Feb 13;57(6):925-934. doi: 10.1021/acs.biochem.7b01124. Epub, 2018 Jan 26. PMID:29314830<ref>PMID:29314830</ref>

-	~~Description: X-ray structure~~ of the ~~proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val~~-~~Arg~~-~~Amba~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: Dahms, S.O]]	+	<div class="pdbe-citations 6eqv" style="background-color:#fffaf0;"></div>
-	[[Category: Than, M.E]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Furin]]
		+	[[Category: Dahms, S O]]
		+	[[Category: Than, M E]]
		+	[[Category: Citrullin]]
		+	[[Category: Complex]]
		+	[[Category: Hydrolase]]
		+	[[Category: Inhibitor]]
		+	[[Category: Proprotein convertase]]
		+	[[Category: Protease]]

OCA at 07:15, 10 January 2018

OCA — Wed, 10 Jan 2018 07:15:41 GMT

←Older revision		Revision as of 07:15, 10 January 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6eqv is ON HOLD	+	The entry 6eqv is ON HOLD until Paper Publication

	Authors: Dahms, S.O., Than, M.E.		Authors: Dahms, S.O., Than, M.E.

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

OCA — Wed, 25 Oct 2017 05:57:41 GMT

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

←Older revision

Revision as of 05:57, 25 October 2017

OCA: New page: '''Unreleased structure''' The entry 6eqv is ON HOLD Authors: Dahms, S.O., Than, M.E. Description: X-ray structure of the proprotein convertase furin bound with the competitive inhibit...

OCA — Wed, 25 Oct 2017 05:57:40 GMT

New page: '''Unreleased structure''' The entry 6eqv is ON HOLD Authors: Dahms, S.O., Than, M.E. Description: X-ray structure of the proprotein convertase furin bound with the competitive inhibit...

New page

'''Unreleased structure'''

The entry 6eqv is ON HOLD

Authors: Dahms, S.O., Than, M.E.

Description: X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba
[[Category: Unreleased Structures]]
[[Category: Dahms, S.O]]
[[Category: Than, M.E]]