5sun - Revision history

OCA at 14:18, 6 March 2024

OCA — Wed, 06 Mar 2024 14:18:11 GMT

←Older revision		Revision as of 14:18, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='5sun' size='340' side='right'caption='[[5sun]], [[Resolution\|resolution]] 2.48Å' scene=''>		<StructureSection load='5sun' size='340' side='right'caption='[[5sun]], [[Resolution\|resolution]] 2.48Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sun]] 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=5SUN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5SUN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sun]] 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=5SUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SUN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=70Q:3-BENZYL-N-[3-(DIMETHYLSULFAMOYL)PHENYL]-4-OXO-3,4-DIHYDROPHTHALAZINE-1-CARBOXAMIDE'>70Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <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]] 2.477Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5svn\|5svn]], [[5svo\|5svo]], [[5svf\|5svf]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=70Q:3-BENZYL-N-[3-(DIMETHYLSULFAMOYL)PHENYL]-4-OXO-3,4-DIHYDROPHTHALAZINE-1-CARBOXAMIDE'>70Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDH1, PICD ([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=5sun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sun OCA], [https://pdbe.org/5sun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sun RCSB], [https://www.ebi.ac.uk/pdbsum/5sun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sun 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/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=5sun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sun OCA], [~~http~~://pdbe.org/5sun PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5sun RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5sun PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5sun ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/IDHC_HUMAN IDHC_HUMAN]] Defects in IDH1 are involved in the development of glioma (GLM) [MIM:[~~http~~://omim.org/entry/137800 137800]]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas. Note=Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors.	+	[https://www.uniprot.org/uniprot/IDHC_HUMAN IDHC_HUMAN] Defects in IDH1 are involved in the development of glioma (GLM) [MIM:[https://omim.org/entry/137800 137800]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas. Note=Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors.
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/IDHC_HUMAN IDHC_HUMAN]
-	Oncogenic IDH1 and IDH2 mutations contribute to cancer via production of R-2-hydroxyglutarate (2-HG). Here, we characterize two structurally distinct mutant- and isoform-selective IDH1 inhibitors that inhibit 2-HG production. Both bind to an allosteric pocket on IDH1, yet shape it differently, highlighting the plasticity of this site. Oncogenic IDH1R132H mutation destabilizes an IDH1 "regulatory segment," which otherwise restricts compound access to the allosteric pocket. Regulatory segment destabilization in wild-type IDH1 promotes inhibitor binding, suggesting that destabilization is critical for mutant selectivity. We also report crystal structures of oncogenic IDH2 mutant isoforms, highlighting the fact that the analogous segment of IDH2 is not similarly destabilized. This intrinsic stability of IDH2 may contribute to observed inhibitor IDH1 isoform selectivity. Moreover, discrete residues in the IDH1 allosteric pocket that differ from IDH2 may also guide IDH1 isoform selectivity. These data provide a deeper understanding of how IDH1 inhibitors achieve mutant and isoform selectivity.	+
-		+
-	Allosteric Mutant IDH1 Inhibitors Reveal Mechanisms for IDH1 Mutant and Isoform Selectivity.,Xie X, Baird D, Bowen K, Capka V, Chen J, Chenail G, Cho Y, Dooley J, Farsidjani A, Fortin P, Kohls D, Kulathila R, Lin F, McKay D, Rodrigues L, Sage D, Toure BB, van der Plas S, Wright K, Xu M, Yin H, Levell J, Pagliarini RA Structure. 2017 Mar 7;25(3):~~506-513. doi: 10.1016~~/~~j.str.2016.12.017. Epub 2017, Jan 26. PMID:28132785<ref>PMID:28132785<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 5sun" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
	*[[Isocitrate dehydrogenase 3D structures\|Isocitrate dehydrogenase 3D structures]]		*[[Isocitrate dehydrogenase 3D structures\|Isocitrate dehydrogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kulathila, R]]	+	[[Category: Kulathila R]]
-	[[Category: Xie, X]]	+	[[Category: Xie X]]
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Isocitrate dehydrogenase]]~~	+
-	~~[[Category: Nadph]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 11:11, 16 September 2020

OCA — Wed, 16 Sep 2020 11:11:38 GMT

←Older revision		Revision as of 11:11, 16 September 2020
Line 1:		Line 1:

	==IDH1 R132H in complex with IDH146==		==IDH1 R132H in complex with IDH146==
-	<StructureSection load='5sun' size='340' side='right' caption='[[5sun]], [[Resolution\|resolution]] 2.48Å' scene=''>	+	<StructureSection load='5sun' size='340' side='right'caption='[[5sun]], [[Resolution\|resolution]] 2.48Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sun]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5SUN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sun]] 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=5SUN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5SUN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70Q:3-BENZYL-N-[3-(DIMETHYLSULFAMOYL)PHENYL]-4-OXO-3,4-DIHYDROPHTHALAZINE-1-CARBOXAMIDE'>70Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <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" id="ligandDat"><scene name='pdbligand=70Q:3-BENZYL-N-[3-(DIMETHYLSULFAMOYL)PHENYL]-4-OXO-3,4-DIHYDROPHTHALAZINE-1-CARBOXAMIDE'>70Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5svn\|5svn]], [[5svo\|5svo]], [[5svf\|5svf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5svn\|5svn]], [[5svo\|5svo]], [[5svf\|5svf]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDH1, PICD ([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/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=5sun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sun OCA], [http://pdbe.org/5sun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sun RCSB], [http://www.ebi.ac.uk/pdbsum/5sun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sun 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=5sun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sun OCA], [http://pdbe.org/5sun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sun RCSB], [http://www.ebi.ac.uk/pdbsum/5sun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sun ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5sun" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sun" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Isocitrate dehydrogenase 3D structures\|Isocitrate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Kulathila, R]]		[[Category: Kulathila, R]]
	[[Category: Xie, X]]		[[Category: Xie, X]]

OCA at 09:28, 10 March 2017

OCA — Fri, 10 Mar 2017 09:28:06 GMT

←Older revision		Revision as of 09:28, 10 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5sun is ~~ON HOLD until Paper~~ Publication	+	==IDH1 R132H in complex with IDH146==
		+	<StructureSection load='5sun' size='340' side='right' caption='[[5sun]], [[Resolution\|resolution]] 2.48Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5sun]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SUN FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70Q:3-BENZYL-N-[3-(DIMETHYLSULFAMOYL)PHENYL]-4-OXO-3,4-DIHYDROPHTHALAZINE-1-CARBOXAMIDE'>70Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5svn\|5svn]], [[5svo\|5svo]], [[5svf\|5svf]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=5sun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sun OCA], [http://pdbe.org/5sun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sun RCSB], [http://www.ebi.ac.uk/pdbsum/5sun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sun ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/IDHC_HUMAN IDHC_HUMAN]] Defects in IDH1 are involved in the development of glioma (GLM) [MIM:[http://omim.org/entry/137800 137800]]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas. Note=Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Oncogenic IDH1 and IDH2 mutations contribute to cancer via production of R-2-hydroxyglutarate (2-HG). Here, we characterize two structurally distinct mutant- and isoform-selective IDH1 inhibitors that inhibit 2-HG production. Both bind to an allosteric pocket on IDH1, yet shape it differently, highlighting the plasticity of this site. Oncogenic IDH1R132H mutation destabilizes an IDH1 "regulatory segment," which otherwise restricts compound access to the allosteric pocket. Regulatory segment destabilization in wild-type IDH1 promotes inhibitor binding, suggesting that destabilization is critical for mutant selectivity. We also report crystal structures of oncogenic IDH2 mutant isoforms, highlighting the fact that the analogous segment of IDH2 is not similarly destabilized. This intrinsic stability of IDH2 may contribute to observed inhibitor IDH1 isoform selectivity. Moreover, discrete residues in the IDH1 allosteric pocket that differ from IDH2 may also guide IDH1 isoform selectivity. These data provide a deeper understanding of how IDH1 inhibitors achieve mutant and isoform selectivity.

-	~~Authors: Xie~~, X., ~~Kulathila~~, R.	+	Allosteric Mutant IDH1 Inhibitors Reveal Mechanisms for IDH1 Mutant and Isoform Selectivity.,Xie X, Baird D, Bowen K, Capka V, Chen J, Chenail G, Cho Y, Dooley J, Farsidjani A, Fortin P, Kohls D, Kulathila R, Lin F, McKay D, Rodrigues L, Sage D, Toure BB, van der Plas S, Wright K, Xu M, Yin H, Levell J, Pagliarini RA Structure. 2017 Mar 7;25(3):506-513. doi: 10.1016/j.str.2016.12.017. Epub 2017, Jan 26. PMID:28132785<ref>PMID:28132785</ref>

-	~~Description: IDH1 R132H in complex with IDH146~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category~~: ~~Xie, X]]~~	+	<div class="pdbe-citations 5sun" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Kulathila, R]]		[[Category: Kulathila, R]]
		+	[[Category: Xie, X]]
		+	[[Category: Inhibitor]]
		+	[[Category: Isocitrate dehydrogenase]]
		+	[[Category: Nadph]]
		+	[[Category: Oxidoreductase]]

OCA at 16:34, 15 December 2016

OCA — Thu, 15 Dec 2016 16:34:21 GMT

←Older revision		Revision as of 16:34, 15 December 2016
Line 5:		Line 5:
	Authors: Xie, X., Kulathila, R.		Authors: Xie, X., Kulathila, R.

-	Description: IDH1 R132H ~~mutant~~ in complex with ~~compound 1~~	+	Description: IDH1 R132H in complex with IDH146
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Xie, X]]		[[Category: Xie, X]]
	[[Category: Kulathila, R]]		[[Category: Kulathila, R]]

OCA at 11:56, 21 September 2016

OCA — Wed, 21 Sep 2016 11:56:59 GMT

←Older revision		Revision as of 11:56, 21 September 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Xie, X., Kulathila, R.		Authors: Xie, X., Kulathila, R.

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

OCA — Wed, 10 Aug 2016 14:42:49 GMT

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

←Older revision

Revision as of 14:42, 10 August 2016

OCA: New page: '''Unreleased structure''' The entry 5sun is ON HOLD Authors: Xie, X., Kulathila, R. Description: IDH1 R132H mutant in complex with compound 1 Category: Unreleased Structures [[Cat...

OCA — Wed, 10 Aug 2016 14:42:47 GMT

New page: '''Unreleased structure''' The entry 5sun is ON HOLD Authors: Xie, X., Kulathila, R. Description: IDH1 R132H mutant in complex with compound 1 Category: Unreleased Structures [[Cat...

New page

'''Unreleased structure'''

The entry 5sun is ON HOLD

Authors: Xie, X., Kulathila, R.

Description: IDH1 R132H mutant in complex with compound 1
[[Category: Unreleased Structures]]
[[Category: Xie, X]]
[[Category: Kulathila, R]]