4o12 - Revision history

OCA at 12:36, 1 March 2024

2024-03-01T12:36:58Z

←Older revision		Revision as of 12:36, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o12]] is a 2 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=4O12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O12 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o12]] is a 2 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=4O12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O12 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.498Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [https://pdbe.org/4o12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [https://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [https://pdbe.org/4o12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [https://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).		[https://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Prolonged inhibition of nicotinamide phosphoribosyltransferase (NAMPT) is a strategy for targeting cancer metabolism. Many NAMPT inhibitors undergo NAMPT-catalyzed phosphoribosylation (pRib), a property often correlated with their cellular potency. To understand this phenomenon and facilitate drug design, we analyzed a potent cellularly active NAMPT inhibitor (GNE-617). A crystal structure of pRib-GNE-617 in complex with NAMPT protein revealed a relaxed binding mode. Consistently, the adduct formation resulted in tight binding and strong product inhibition. In contrast, a biochemically equipotent isomer of GNE-617 (GNE-643) also formed pRib adducts but displayed significantly weaker cytotoxicity. Structural analysis revealed an altered ligand conformation of GNE-643, thus suggesting weak association of the adducts with NAMPT. Our data support a model for cellularly active NAMPT inhibitors that undergo NAMPT-catalyzed phosphoribosylation to produce pRib adducts that retain efficient binding to the enzyme.
-
-	Structural and biochemical analyses of the catalysis and potency impact of inhibitor phosphoribosylation by human nicotinamide phosphoribosyltransferase.,Oh A, Ho YC, Zak M, Liu Y, Chen X, Yuen PW, Zheng X, Liu Y, Dragovich PS, Wang W Chembiochem. 2014 May 26;15(8):1121-30. doi: 10.1002/cbic.201402023. Epub 2014, May 5. PMID:24797455<ref>PMID:24797455</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4o12" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Phosphoribosyltransferase 3D structures\|Phosphoribosyltransferase 3D structures]]		*[[Phosphoribosyltransferase 3D structures\|Phosphoribosyltransferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:51, 18 January 2023

2023-01-18T08:51:08Z

←Older revision		Revision as of 08:51, 18 January 2023
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	<StructureSection load='4o12' size='340' side='right'caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4o12' size='340' side='right'caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o12]] 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=4O12 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O12 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o12]] is a 2 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=4O12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O12 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [https://pdbe.org/4o12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [https://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NAMPT, PBEF, PBEF1 ([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/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [~~http~~://pdbe.org/4o12 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN]] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).	+	[https://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]	+	*[[Phosphoribosyltransferase 3D structures\|Phosphoribosyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Nicotinamide phosphoribosyltransferase]]~~	+	[[Category: Oh A]]
-	[[Category: Oh, A]]	+	[[Category: Wang W]]
-	[[Category: Wang, W]]	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 08:58, 10 April 2019

2019-04-10T08:58:52Z

←Older revision		Revision as of 08:58, 10 April 2019
Line 1:		Line 1:

	==Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase==		==Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase==
-	<StructureSection load='4o12' size='340' side='right' caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4o12' size='340' side='right'caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O12 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o12]] 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=4O12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O12 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NAMPT, PBEF, PBEF1 ([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/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://pdbe.org/4o12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://pdbe.org/4o12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 ProSAT]</span></td></tr>
Line 27:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Nicotinamide phosphoribosyltransferase]]		[[Category: Nicotinamide phosphoribosyltransferase]]
	[[Category: Oh, A]]		[[Category: Oh, A]]
	[[Category: Wang, W]]		[[Category: Wang, W]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 15:24, 4 August 2016

2016-08-04T15:24:39Z

←Older revision		Revision as of 15:24, 4 August 2016
Line 1:		Line 1:
		+
	==Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase==		==Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase==
	<StructureSection load='4o12' size='340' side='right' caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4o12' size='340' side='right' caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum]</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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://pdbe.org/4o12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o12 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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>
	</div>		</div>
		+	<div class="pdbe-citations 4o12" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:32, 25 December 2014

2014-12-25T10:32:05Z

←Older revision		Revision as of 10:32, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O12 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O12 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum]</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=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN]] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Nicotinamide phosphoribosyltransferase]]		[[Category: Nicotinamide phosphoribosyltransferase]]
-	[[Category: Oh, A.]]	+	[[Category: Oh, A]]
-	[[Category: Wang, W.]]	+	[[Category: Wang, W]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 07:48, 18 June 2014

2014-06-18T07:48:11Z

←Older revision		Revision as of 07:48, 18 June 2014
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-	'''~~Unreleased~~ structure'''	+	==Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase==
		+	<StructureSection load='4o12' size='340' side='right' caption='[[4o12]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4o12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O12 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QG:2-[6-(4-CHLOROPHENOXY)HEXYL]-1-CYANO-3-PYRIDIN-4-YLGUANIDINE'>2QG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0z\|4o0z]], [[4o10\|4o10]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o12 RCSB], [http://www.ebi.ac.uk/pdbsum/4o12 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Prolonged inhibition of nicotinamide phosphoribosyltransferase (NAMPT) is a strategy for targeting cancer metabolism. Many NAMPT inhibitors undergo NAMPT-catalyzed phosphoribosylation (pRib), a property often correlated with their cellular potency. To understand this phenomenon and facilitate drug design, we analyzed a potent cellularly active NAMPT inhibitor (GNE-617). A crystal structure of pRib-GNE-617 in complex with NAMPT protein revealed a relaxed binding mode. Consistently, the adduct formation resulted in tight binding and strong product inhibition. In contrast, a biochemically equipotent isomer of GNE-617 (GNE-643) also formed pRib adducts but displayed significantly weaker cytotoxicity. Structural analysis revealed an altered ligand conformation of GNE-643, thus suggesting weak association of the adducts with NAMPT. Our data support a model for cellularly active NAMPT inhibitors that undergo NAMPT-catalyzed phosphoribosylation to produce pRib adducts that retain efficient binding to the enzyme.

-	~~The entry 4o12 is ON HOLD until Paper Publication~~	+	Structural and biochemical analyses of the catalysis and potency impact of inhibitor phosphoribosylation by human nicotinamide phosphoribosyltransferase.,Oh A, Ho YC, Zak M, Liu Y, Chen X, Yuen PW, Zheng X, Liu Y, Dragovich PS, Wang W Chembiochem. 2014 May 26;15(8):1121-30. doi: 10.1002/cbic.201402023. Epub 2014, May 5. PMID:24797455<ref>PMID:24797455</ref>

-	~~Authors~~: Oh, A., Wang, W.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Nicotinamide phosphoribosyltransferase]]
		+	[[Category: Oh, A.]]
		+	[[Category: Wang, W.]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 04:49, 13 February 2014

2014-02-13T04:49:08Z

←Older revision		Revision as of 04:49, 13 February 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o12 is ON HOLD	+	The entry 4o12 is ON HOLD until Paper Publication

	Authors: Oh, A., Wang, W.		Authors: Oh, A., Wang, W.

	Description: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase		Description: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase

OCA: Protected "4o12" [edit=sysop:move=sysop]

2013-12-25T09:29:47Z

Protected "4o12" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:29, 25 December 2013

OCA: New page: '''Unreleased structure''' The entry 4o12 is ON HOLD Authors: Oh, A., Wang, W. Description: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phospho...

2013-12-25T09:29:46Z

New page: '''Unreleased structure''' The entry 4o12 is ON HOLD Authors: Oh, A., Wang, W. Description: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phospho...

New page

'''Unreleased structure'''

The entry 4o12 is ON HOLD

Authors: Oh, A., Wang, W.

Description: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase