5k7y - Revision history

OCA at 10:42, 27 September 2023

OCA — Wed, 27 Sep 2023 10:42:57 GMT

←Older revision		Revision as of 10:42, 27 September 2023
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	<StructureSection load='5k7y' size='340' side='right'caption='[[5k7y]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='5k7y' size='340' side='right'caption='[[5k7y]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k7y]] is a 1 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=5K7Y OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5K7Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k7y]] is a 1 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=5K7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K7Y FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.79Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>NT5C2, NT5B, NT5CP, PNT5 ([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=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5]~~ </~~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=5k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7y OCA], [https://pdbe.org/5k7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k7y RCSB], [https://www.ebi.ac.uk/pdbsum/5k7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7y 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=5k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7y OCA], [~~http~~://pdbe.org/5k7y PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5k7y RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5k7y PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7y ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] Autosomal recessive spastic paraplegia type 45. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:24482476</ref>	+	[https://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN] Autosomal recessive spastic paraplegia type 45. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:24482476</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.	+	[https://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN] May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.
	<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: ~~5'-nucleotidase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hnizda, A]]	+	[[Category: Hnizda A]]
-	[[Category: Pachl, P]]	+	[[Category: Pachl P]]
-	[[Category: Rezacova, P]]	+	[[Category: Rezacova P]]
-	[[Category: Skerlova, J]]	+	[[Category: Skerlova J]]
-	~~[[Category: Enzyme]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Purine~~]]	+

OCA at 09:25, 1 July 2020

OCA — Wed, 01 Jul 2020 09:25:42 GMT

←Older revision		Revision as of 09:25, 1 July 2020
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	==Crystal structure of enzyme in purine metabolism==		==Crystal structure of enzyme in purine metabolism==
-	<StructureSection load='5k7y' size='340' side='right' caption='[[5k7y]], [[Resolution\|resolution]] 1.79Å' scene=''>	+	<StructureSection load='5k7y' size='340' side='right'caption='[[5k7y]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k7y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K7Y OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5K7Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k7y]] is a 1 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=5K7Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K7Y FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NT5C2, NT5B, NT5CP, PNT5 ([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/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </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=5k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7y OCA], [http://pdbe.org/5k7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k7y RCSB], [http://www.ebi.ac.uk/pdbsum/5k7y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7y 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=5k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7y OCA], [http://pdbe.org/5k7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k7y RCSB], [http://www.ebi.ac.uk/pdbsum/5k7y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7y ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</StructureSection>		</StructureSection>
	[[Category: 5'-nucleotidase]]		[[Category: 5'-nucleotidase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hnizda, A]]		[[Category: Hnizda, A]]
	[[Category: Pachl, P]]		[[Category: Pachl, P]]

OCA at 10:59, 2 November 2016

OCA — Wed, 02 Nov 2016 10:59:09 GMT

←Older revision		Revision as of 10:59, 2 November 2016
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.		[[http://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: Relapsed acute lymphoblastic leukemia (ALL) is one of the main causes of mortality in childhood malignancies. Previous genetic studies demonstrated that chemoresistant ALL is driven by activating mutations in NT5C2, the gene encoding cytosolic 5 -nucleotidase (cN-II). However, molecular mechanisms underlying this hyperactivation are still unknown. Here, we present kinetic and structural properties of cN-II variants that represent 75 % of mutated alleles in patients who experience relapsed ALL (R367Q, R238W and L375F). RESULTS: Enzyme kinetics measurements revealed that the mutants are consitutively active without need for allosteric activators. This shows that hyperactivity is not caused by a direct catalytic effect but rather by misregulation of cN-II. X-ray crystallography combined with mass spectrometry-based techniques demonstrated that this misregulation is driven by structural modulation of the oligomeric interface within the cN-II homotetrameric assembly. These specific conformational changes are shared between the studied variants, despite the relatively random spatial distribution of the mutations. CONCLUSIONS: These findings define a common molecular mechanism for cN-II hyperactivity, which provides a solid basis for targeted therapy of leukemia. Our study highlights the cN-II oligomerization interface as an attractive pharmacological target.
		+
		+	Oligomeric interface modulation causes misregulation of purine 5 -nucleotidase in relapsed leukemia.,Hnizda A, Skerlova J, Fabry M, Pachl P, Sinalova M, Vrzal L, Man P, Novak P, Rezacova P, Veverka V BMC Biol. 2016 Oct 19;14(1):91. PMID:27756303<ref>PMID:27756303</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5k7y" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:55, 21 September 2016

OCA — Wed, 21 Sep 2016 13:55:20 GMT

←Older revision		Revision as of 13:55, 21 September 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5k7y is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of enzyme in purine metabolism==
-		+	<StructureSection load='5k7y' size='340' side='right' caption='[[5k7y]], [[Resolution\|resolution]] 1.79Å' scene=''>
-	~~Authors~~: ~~Skerlova~~, J., ~~Hnizda~~, A., ~~Pachl~~, P., ~~Rezacova, P~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5k7y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K7Y FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~enzyme~~ in purine ~~metabolism~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </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=5k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7y OCA], [http://pdbe.org/5k7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k7y RCSB], [http://www.ebi.ac.uk/pdbsum/5k7y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7y ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] Autosomal recessive spastic paraplegia type 45. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:24482476</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/5NTC_HUMAN 5NTC_HUMAN]] May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: 5'-nucleotidase]]
	[[Category: Hnizda, A]]		[[Category: Hnizda, A]]
	[[Category: Pachl, P]]		[[Category: Pachl, P]]
	[[Category: Rezacova, P]]		[[Category: Rezacova, P]]
	[[Category: Skerlova, J]]		[[Category: Skerlova, J]]
		+	[[Category: Enzyme]]
		+	[[Category: Hydrolase]]
		+	[[Category: Purine]]

OCA at 13:31, 20 June 2016

OCA — Mon, 20 Jun 2016 13:31:47 GMT

←Older revision		Revision as of 13:31, 20 June 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5k7y is ON HOLD	+	The entry 5k7y is ON HOLD until Paper Publication

-	Authors: Skerlova ~~Jana~~, Hnizda ~~Ales~~, Pachl ~~Petr~~, Rezacova ~~Pavlina~~	+	Authors: Skerlova, J., Hnizda, A., Pachl, P., Rezacova, P.

	Description: Crystal structure of enzyme in purine metabolism		Description: Crystal structure of enzyme in purine metabolism
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Skerlova Jana,~~ Hnizda ~~Ales~~, Pachl ~~Petr~~, Rezacova ~~Pavlina~~]]	+	[[Category: Hnizda, A]]
		+	[[Category: Pachl, P]]
		+	[[Category: Rezacova, P]]
		+	[[Category: Skerlova, J]]

OCA: Protected "5k7y" [edit=sysop:move=sysop]

OCA — Wed, 01 Jun 2016 14:26:50 GMT

Protected "5k7y" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:26, 1 June 2016

OCA: New page: '''Unreleased structure''' The entry 5k7y is ON HOLD Authors: Skerlova Jana, Hnizda Ales, Pachl Petr, Rezacova Pavlina Description: Crystal structure of enzyme in purine metabolism [[C...

OCA — Wed, 01 Jun 2016 14:26:49 GMT

New page: '''Unreleased structure''' The entry 5k7y is ON HOLD Authors: Skerlova Jana, Hnizda Ales, Pachl Petr, Rezacova Pavlina Description: Crystal structure of enzyme in purine metabolism [[C...

New page

'''Unreleased structure'''

The entry 5k7y is ON HOLD

Authors: Skerlova Jana, Hnizda Ales, Pachl Petr, Rezacova Pavlina

Description: Crystal structure of enzyme in purine metabolism
[[Category: Unreleased Structures]]
[[Category: Skerlova Jana, Hnizda Ales, Pachl Petr, Rezacova Pavlina]]