5my8 - Revision history

OCA at 17:53, 8 November 2023

OCA — Wed, 08 Nov 2023 17:53:49 GMT

←Older revision		Revision as of 17:53, 8 November 2023
Line 3:		Line 3:
	<StructureSection load='5my8' size='340' side='right'caption='[[5my8]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='5my8' size='340' side='right'caption='[[5my8]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5my8]] 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=5MY8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5MY8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5my8]] 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=5MY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MY8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RXZ:SPHINX31'>RXZ</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]] 1.7Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SRPK1 ([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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RXZ:SPHINX31'>RXZ</scene></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=5my8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my8 OCA], [~~http~~://pdbe.org/5my8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5my8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5my8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5my8 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=5my8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my8 OCA], [https://pdbe.org/5my8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5my8 RCSB], [https://www.ebi.ac.uk/pdbsum/5my8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5my8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SRPK1_HUMAN SRPK1_HUMAN]] Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.<ref>PMID:8208298</ref> <ref>PMID:11509566</ref> <ref>PMID:12134018</ref> <ref>PMID:15034300</ref> <ref>PMID:9237760</ref> <ref>PMID:10049757</ref> <ref>PMID:10390541</ref> <ref>PMID:14555757</ref> <ref>PMID:16122776</ref> <ref>PMID:18155240</ref> <ref>PMID:18687337</ref> <ref>PMID:19886675</ref> <ref>PMID:19240134</ref> <ref>PMID:19477182</ref> <ref>PMID:20708644</ref> <ref>PMID:16209947</ref>	+	[https://www.uniprot.org/uniprot/SRPK1_HUMAN SRPK1_HUMAN] Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.<ref>PMID:8208298</ref> <ref>PMID:11509566</ref> <ref>PMID:12134018</ref> <ref>PMID:15034300</ref> <ref>PMID:9237760</ref> <ref>PMID:10049757</ref> <ref>PMID:10390541</ref> <ref>PMID:14555757</ref> <ref>PMID:16122776</ref> <ref>PMID:18155240</ref> <ref>PMID:18687337</ref> <ref>PMID:19886675</ref> <ref>PMID:19240134</ref> <ref>PMID:19477182</ref> <ref>PMID:20708644</ref> <ref>PMID:16209947</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Chaikuad, A]]	+	[[Category: Chaikuad A]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Knapp S]]
-	[[Category: Knapp, S]]	+	[[Category: Von Delft F]]
-	[[Category: ~~Structural genomic]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Sgc]]~~	+
-	~~[[Category: Splicing kinase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:32, 19 August 2020

OCA — Wed, 19 Aug 2020 07:32:03 GMT

←Older revision		Revision as of 07:32, 19 August 2020
Line 1:		Line 1:

	==Crystal structure of SRPK1 in complex with SPHINX31==		==Crystal structure of SRPK1 in complex with SPHINX31==
-	<StructureSection load='5my8' size='340' side='right' caption='[[5my8]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='5my8' size='340' side='right'caption='[[5my8]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5my8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MY8 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5MY8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5my8]] 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=5MY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MY8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RXZ:SPHINX31'>RXZ</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RXZ:SPHINX31'>RXZ</scene></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=5my8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my8 OCA], [http://pdbe.org/5my8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5my8 RCSB], [http://www.ebi.ac.uk/pdbsum/5my8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5my8 ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SRPK1 ([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=5my8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my8 OCA], [http://pdbe.org/5my8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5my8 RCSB], [http://www.ebi.ac.uk/pdbsum/5my8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5my8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Bountra, C]]		[[Category: Bountra, C]]

OCA at 12:50, 10 May 2017

OCA — Wed, 10 May 2017 12:50:40 GMT

←Older revision		Revision as of 12:50, 10 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5my8 is ~~ON HOLD~~	+	==Crystal structure of SRPK1 in complex with SPHINX31==
		+	<StructureSection load='5my8' size='340' side='right' caption='[[5my8]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5my8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MY8 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RXZ:SPHINX31'>RXZ</scene></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=5my8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my8 OCA], [http://pdbe.org/5my8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5my8 RCSB], [http://www.ebi.ac.uk/pdbsum/5my8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5my8 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SRPK1_HUMAN SRPK1_HUMAN]] Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.<ref>PMID:8208298</ref> <ref>PMID:11509566</ref> <ref>PMID:12134018</ref> <ref>PMID:15034300</ref> <ref>PMID:9237760</ref> <ref>PMID:10049757</ref> <ref>PMID:10390541</ref> <ref>PMID:14555757</ref> <ref>PMID:16122776</ref> <ref>PMID:18155240</ref> <ref>PMID:18687337</ref> <ref>PMID:19886675</ref> <ref>PMID:19240134</ref> <ref>PMID:19477182</ref> <ref>PMID:20708644</ref> <ref>PMID:16209947</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Serine/arginine-protein kinase 1 (SRPK1) regulates alternative splicing of VEGF-A to pro-angiogenic isoforms and SRPK1 inhibition can restore the balance of pro/antiangiogenic isoforms to normal physiological levels. The lack of potency and selectivity of available compounds has limited development of SRPK1 inhibitors, with the control of alternative splicing by splicing factor-specific kinases yet to be translated. We present here compounds that occupy a binding pocket created by the unique helical insert of SRPK1, and trigger a backbone flip in the hinge region, that results in potent (<10 nM) and selective inhibition of SRPK1 kinase activity. Treatment with these inhibitors inhibited SRPK1 activity and phosphorylation of serine/arginine splicing factor 1 (SRSF1), resulting in alternative splicing of VEGF-A from pro-angiogenic to antiangiogenic isoforms. This property resulted in potent inhibition of blood vessel growth in models of choroidal angiogenesis in vivo. This work identifies tool compounds for splice isoform selective targeting of pro-angiogenic VEGF, which may lead to new therapeutic strategies for a diversity of diseases where dysfunctional splicing drives disease development.

-	~~Authors: Chaikuad~~, A., ~~von Delft~~, F., ~~Bountra~~, C., ~~Arrowsmith~~, C~~.H.~~, ~~Edwards~~, ~~A.M.~~, ~~Knapp~~, S., ~~Structural Genomics Consortium~~ (~~SGC~~)	+	Development of Potent, Selective SRPK1 Inhibitors as Potential Topical Therapeutics for Neovascular Eye Disease.,Batson J, Toop HD, Redondo C, Babaei-Jadidi R, Chaikuad A, Wearmouth SF, Gibbons B, Allen C, Tallant C, Zhang J, Du C, Hancox JC, Hawtrey T, Da Rocha J, Griffith R, Knapp S, Bates DO, Morris JC ACS Chem Biol. 2017 Mar 17;12(3):825-832. doi: 10.1021/acschembio.6b01048. Epub, 2017 Feb 6. PMID:28135068<ref>PMID:28135068</ref>

-	~~Description: Crystal structure~~ of ~~SRPK1 in complex with SPHINX31~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5my8" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Arrowsmith, C H]]
		+	[[Category: Bountra, C]]
	[[Category: Chaikuad, A]]		[[Category: Chaikuad, A]]
-	[[Category: ~~Arrowsmith~~, ~~C.H~~]]	+	[[Category: Delft, F von]]
-	[[Category: ~~Von Delft~~, F]]	+	[[Category: Edwards, A M]]
	[[Category: Knapp, S]]		[[Category: Knapp, S]]
-	[[Category: ~~Edwards, A.M~~]]	+	[[Category: Structural genomic]]
-	[[Category: ~~Structural Genomics Consortium (~~Sgc)]]	+	[[Category: Inhibitor]]
-	[[Category: ~~Bountra, C~~]]	+	[[Category: Sgc]]
		+	[[Category: Splicing kinase]]
		+	[[Category: Transferase]]

OCA at 11:47, 9 March 2017

OCA — Thu, 09 Mar 2017 11:47:10 GMT

←Older revision		Revision as of 11:47, 9 March 2017
Line 3:		Line 3:
	The entry 5my8 is ON HOLD		The entry 5my8 is ON HOLD

-	Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium	+	Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium (SGC)

	Description: Crystal structure of SRPK1 in complex with SPHINX31		Description: Crystal structure of SRPK1 in complex with SPHINX31
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Chaikuad, A]]		[[Category: Chaikuad, A]]
-	[[Category: Knapp, S]]
-	[[Category: Bountra, C]]
	[[Category: Arrowsmith, C.H]]		[[Category: Arrowsmith, C.H]]
	[[Category: Von Delft, F]]		[[Category: Von Delft, F]]
		+	[[Category: Knapp, S]]
	[[Category: Edwards, A.M]]		[[Category: Edwards, A.M]]
-	[[Category: Structural Genomics Consortium]]	+	[[Category: Structural Genomics Consortium (Sgc)]]
		+	[[Category: Bountra, C]]

OCA: Protected "5my8" [edit=sysop:move=sysop]

OCA — Wed, 01 Feb 2017 15:24:07 GMT

Protected "5my8" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:24, 1 February 2017

OCA: New page: '''Unreleased structure''' The entry 5my8 is ON HOLD Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium Descr...

OCA — Wed, 01 Feb 2017 15:24:05 GMT

New page: '''Unreleased structure''' The entry 5my8 is ON HOLD Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium Descr...

New page

'''Unreleased structure'''

The entry 5my8 is ON HOLD

Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium

Description: Crystal structure of SRPK1 in complex with SPHINX31
[[Category: Unreleased Structures]]
[[Category: Chaikuad, A]]
[[Category: Knapp, S]]
[[Category: Bountra, C]]
[[Category: Arrowsmith, C.H]]
[[Category: Von Delft, F]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium]]