6xrm - Revision history

OCA at 14:51, 6 March 2024

OCA — Wed, 06 Mar 2024 14:51:23 GMT

←Older revision		Revision as of 14:51, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='6xrm' size='340' side='right'caption='[[6xrm]], [[Resolution\|resolution]] 2.88Å' scene=''>		<StructureSection load='6xrm' size='340' side='right'caption='[[6xrm]], [[Resolution\|resolution]] 2.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6xrm]] 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=6XRM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6XRM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6xrm]] 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=6XRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XRM FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V81:5-[2-amino-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl]-2-[(1S)-1-cyclopropylethyl]-7-(trifluoromethyl)-2,3-dihydro-1H-isoindol-1-one'>V81</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]] 2.88Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6xrl\|6xrl]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V81:5-[2-amino-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl]-2-[(1S)-1-cyclopropylethyl]-7-(trifluoromethyl)-2,3-dihydro-1H-isoindol-1-one'>V81</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIK3CG ([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=6xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrm OCA], [https://pdbe.org/6xrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xrm RCSB], [https://www.ebi.ac.uk/pdbsum/6xrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrm 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=6xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrm OCA], [~~http~~://pdbe.org/6xrm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6xrm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6xrm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrm ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PK3CG_HUMAN PK3CG_HUMAN]] Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.<ref>PMID:7624799</ref> <ref>PMID:12163475</ref> <ref>PMID:15294162</ref> <ref>PMID:16094730</ref> <ref>PMID:21393242</ref>	+	[https://www.uniprot.org/uniprot/PK3CG_HUMAN PK3CG_HUMAN] Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.<ref>PMID:7624799</ref> <ref>PMID:12163475</ref> <ref>PMID:15294162</ref> <ref>PMID:16094730</ref> <ref>PMID:21393242</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The selective inhibition of the lipid signaling enzyme PI3Kgamma constitutes an opportunity to mediate immunosuppression and inflammation within the tumor microenvironment but is difficult to achieve due to the high sequence homology across the class 1 PI3K isoforms. Here, we describe the design of a novel series of potent PI3Kgamma inhibitors that attain high isoform selectivity through the divergent projection of substituents into both the 'selectivity' and 'alkyl-induced' pockets within the ATP binding site of PI3Kgamma. These efforts have culminated in the discovery of 5-[2-amino-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl]-2-[(1S)-1-c yclopropylethyl]-7-(trifluoromethyl)-2,3-dihydro-1H-isoindol-1-one (4, IC50 = 0.064 microM, THP-1 cells), which displays >700-fold selectivity for PI3Kgamma over the other class I isoforms and is a promising step towards the identification of a clinical development candidate. The structure-activity relationships identified throughout this campaign demonstrate that greater gamma-selectivity can be achieved by inhibitors that occupy an 'alkyl-induced' pocket and possess bicyclic hinge-binding motifs capable of forming more than one hydrogen bond to the hinge region of PI3Kgamma.	+
-		+
-	Discovery of Potent and Selective PI3Kgamma Inhibitors.,Drew SL, Thomas-Tran R, Beatty JW, Fournier J, Lawson KV, Miles DH, Mata G, Sharif EU, Yan X, Mailyan AK, Ginn E, Chen J, Wong K, Soni D, Dhanota P, Chen PY, Shaqfeh SG, Meleza C, Pham AT, Chen A, Zhao X, Banuelos J, Jin L, Schindler U, Walters MJ, Young SW, Walker NP, Leleti MR, Powers JP, Jeffrey JL J Med Chem. 2020 Aug 31. doi: 10.1021/acs.jmedchem.0c01203. PMID:32865410<ref>PMID:32865410</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6xrm" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 27:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Jeffrey~~, J L~~]]	+	[[Category: Jeffrey JL]]
-	[[Category: Walker~~, N P]]~~	+	[[Category: Walker NP]]
-	~~[[Category: Cancer]]~~	+
-	~~[[Category: Immunosuppression]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Phosphoinositide 3-kinase gamma]]~~	+
-	~~[[Category: Protero]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 08:40, 21 October 2020

OCA — Wed, 21 Oct 2020 08:40:34 GMT

←Older revision		Revision as of 08:40, 21 October 2020
Line 1:		Line 1:

	==Crystal structure of human PI3K-gamma in complex with Compound 4==		==Crystal structure of human PI3K-gamma in complex with Compound 4==
-	<StructureSection load='6xrm' size='340' side='right'caption='[[6xrm]]' scene=''>	+	<StructureSection load='6xrm' size='340' side='right'caption='[[6xrm]], [[Resolution\|resolution]] 2.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XRM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XRM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6xrm]] 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=6XRM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XRM FirstGlance]. <br>
-	</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=6xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrm OCA], [http://pdbe.org/6xrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xrm RCSB], [http://www.ebi.ac.uk/pdbsum/6xrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrm ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V81:5-[2-amino-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl]-2-[(1S)-1-cyclopropylethyl]-7-(trifluoromethyl)-2,3-dihydro-1H-isoindol-1-one'>V81</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6xrl\|6xrl]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIK3CG ([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'>[http://proteopedia.org/fgij/fg.htm?mol=6xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrm OCA], [http://pdbe.org/6xrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xrm RCSB], [http://www.ebi.ac.uk/pdbsum/6xrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrm ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PK3CG_HUMAN PK3CG_HUMAN]] Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.<ref>PMID:7624799</ref> <ref>PMID:12163475</ref> <ref>PMID:15294162</ref> <ref>PMID:16094730</ref> <ref>PMID:21393242</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The selective inhibition of the lipid signaling enzyme PI3Kgamma constitutes an opportunity to mediate immunosuppression and inflammation within the tumor microenvironment but is difficult to achieve due to the high sequence homology across the class 1 PI3K isoforms. Here, we describe the design of a novel series of potent PI3Kgamma inhibitors that attain high isoform selectivity through the divergent projection of substituents into both the 'selectivity' and 'alkyl-induced' pockets within the ATP binding site of PI3Kgamma. These efforts have culminated in the discovery of 5-[2-amino-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl]-2-[(1S)-1-c yclopropylethyl]-7-(trifluoromethyl)-2,3-dihydro-1H-isoindol-1-one (4, IC50 = 0.064 microM, THP-1 cells), which displays >700-fold selectivity for PI3Kgamma over the other class I isoforms and is a promising step towards the identification of a clinical development candidate. The structure-activity relationships identified throughout this campaign demonstrate that greater gamma-selectivity can be achieved by inhibitors that occupy an 'alkyl-induced' pocket and possess bicyclic hinge-binding motifs capable of forming more than one hydrogen bond to the hinge region of PI3Kgamma.
		+
		+	Discovery of Potent and Selective PI3Kgamma Inhibitors.,Drew SL, Thomas-Tran R, Beatty JW, Fournier J, Lawson KV, Miles DH, Mata G, Sharif EU, Yan X, Mailyan AK, Ginn E, Chen J, Wong K, Soni D, Dhanota P, Chen PY, Shaqfeh SG, Meleza C, Pham AT, Chen A, Zhao X, Banuelos J, Jin L, Schindler U, Walters MJ, Young SW, Walker NP, Leleti MR, Powers JP, Jeffrey JL J Med Chem. 2020 Aug 31. doi: 10.1021/acs.jmedchem.0c01203. PMID:32865410<ref>PMID:32865410</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6xrm" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoinositide 3-kinase 3D structures\|Phosphoinositide 3-kinase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Jeffrey JL]]	+	[[Category: Jeffrey, J L]]
-	[[Category: Walker NP]]	+	[[Category: Walker, N P]]
		+	[[Category: Cancer]]
		+	[[Category: Immunosuppression]]
		+	[[Category: Inhibitor]]
		+	[[Category: Phosphoinositide 3-kinase gamma]]
		+	[[Category: Protero]]
		+	[[Category: Transferase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 09:50, 16 September 2020

OCA — Wed, 16 Sep 2020 09:50:03 GMT

←Older revision		Revision as of 09:50, 16 September 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6xrm ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of human PI3K-gamma in complex with Compound 4==
-		+	<StructureSection load='6xrm' size='340' side='right'caption='[[6xrm]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XRM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XRM FirstGlance]. <br>
-	~~Description~~:	+	</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=6xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrm OCA], [http://pdbe.org/6xrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xrm RCSB], [http://www.ebi.ac.uk/pdbsum/6xrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrm ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Jeffrey JL]]
		+	[[Category: Walker NP]]

OCA at 09:25, 29 July 2020

OCA — Wed, 29 Jul 2020 09:25:34 GMT

←Older revision		Revision as of 09:25, 29 July 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 22 Jul 2020 06:57:10 GMT

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

←Older revision

Revision as of 06:57, 22 July 2020

OCA: New page: '''Unreleased structure''' The entry 6xrm is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 22 Jul 2020 06:57:08 GMT

New page: '''Unreleased structure''' The entry 6xrm is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6xrm is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]