3rtr - Revision history

OCA at 12:37, 14 March 2024

OCA — Thu, 14 Mar 2024 12:37:05 GMT

←Older revision		Revision as of 12:37, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3rtr' size='340' side='right'caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>		<StructureSection load='3rtr' size='340' side='right'caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RTR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rtr]] is a 8 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=3RTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RTR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.21Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CUL1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN]), RBX1, RNF75, ROC1 ([https~~:/~~/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=ZN:ZINC+ION'>ZN</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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [https://pdbe.org/3rtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [https://www.ebi.ac.uk/pdbsum/3rtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtr 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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [https://pdbe.org/3rtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [https://www.ebi.ac.uk/pdbsum/3rtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CUL1_HUMAN CUL1_HUMAN]] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110 (By similarity).<ref>PMID:9663463</ref> <ref>PMID:15531760</ref> <ref>PMID:15640526</ref> <ref>PMID:18644861</ref> <ref>PMID:19679664</ref> [[https://www.uniprot.org/uniprot/RBX1_HUMAN RBX1_HUMAN]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.<ref>PMID:10579999</ref> <ref>PMID:11027288</ref> <ref>PMID:16751180</ref> <ref>PMID:16678110</ref> <ref>PMID:19679664</ref>	+	[https://www.uniprot.org/uniprot/CUL1_HUMAN CUL1_HUMAN] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110 (By similarity).<ref>PMID:9663463</ref> <ref>PMID:15531760</ref> <ref>PMID:15640526</ref> <ref>PMID:18644861</ref> <ref>PMID:19679664</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.	+
-		+
-	A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.,Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, Kriwacki RW, Schulman BA Nat Struct Mol Biol. 2011 Jul 17;18(8):947-9. doi: 10.1038/nsmb.2086. PMID:21765416<ref>PMID:21765416</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3rtr" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Calabrese~~, M F~~]]	+	[[Category: Calabrese MF]]
-	[[Category: Duda~~, D M~~]]	+	[[Category: Duda DM]]
-	[[Category: Grace~~, C R~~]]	+	[[Category: Grace CR]]
-	[[Category: Kriwacki~~, R W~~]]	+	[[Category: Kriwacki RW]]
-	[[Category: Kurinov, I]]	+	[[Category: Kurinov I]]
-	[[Category: Schulman~~, B A~~]]	+	[[Category: Schulman BA]]
-	[[Category: Scott~~, D C]]~~	+	[[Category: Scott DC]]
-	~~[[Category: Cullin]]~~	+
-	~~[[Category: E3 ligase]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Nedd8]]~~	+
-	~~[[Category: Ubiquitin]]~~	+
-	~~[[Category: Ubl conjugation pathway~~]]	+

OCA at 10:24, 22 June 2022

OCA — Wed, 22 Jun 2022 10:24:53 GMT

←Older revision		Revision as of 10:24, 22 June 2022
Line 1:		Line 1:

	==A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases==		==A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases==
-	<StructureSection load='3rtr' size='340' side='right' caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>	+	<StructureSection load='3rtr' size='340' side='right'caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rtr]] is a 8 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=3RTR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RTR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RTR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RBX1, RNF75, ROC1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RBX1, RNF75, ROC1 ([https://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~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [~~http~~://pdbe.org/3rtr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rtr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtr 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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [https://pdbe.org/3rtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [https://www.ebi.ac.uk/pdbsum/3rtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CUL1_HUMAN CUL1_HUMAN]] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110 (By similarity).<ref>PMID:9663463</ref> <ref>PMID:15531760</ref> <ref>PMID:15640526</ref> <ref>PMID:18644861</ref> <ref>PMID:19679664</ref> [[~~http~~://www.uniprot.org/uniprot/RBX1_HUMAN RBX1_HUMAN]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.<ref>PMID:10579999</ref> <ref>PMID:11027288</ref> <ref>PMID:16751180</ref> <ref>PMID:16678110</ref> <ref>PMID:19679664</ref>	+	[[https://www.uniprot.org/uniprot/CUL1_HUMAN CUL1_HUMAN]] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110 (By similarity).<ref>PMID:9663463</ref> <ref>PMID:15531760</ref> <ref>PMID:15640526</ref> <ref>PMID:18644861</ref> <ref>PMID:19679664</ref> [[https://www.uniprot.org/uniprot/RBX1_HUMAN RBX1_HUMAN]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.<ref>PMID:10579999</ref> <ref>PMID:11027288</ref> <ref>PMID:16751180</ref> <ref>PMID:16678110</ref> <ref>PMID:19679664</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Cullin\|Cullin]]	+	*[[Cullin 3D structures\|Cullin 3D structures]]
-	*[[~~RING~~ box protein\|~~RING~~ box protein]]	+	*[[Ring box protein 3D structures\|Ring box protein 3D structures]]
-	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Calabrese, M F]]		[[Category: Calabrese, M F]]
	[[Category: Duda, D M]]		[[Category: Duda, D M]]

OCA at 14:21, 5 August 2016

OCA — Fri, 05 Aug 2016 14:21:36 GMT

←Older revision		Revision as of 14:21, 5 August 2016
Line 1:		Line 1:
		+
	==A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases==		==A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases==
	<StructureSection load='3rtr' size='340' side='right' caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>		<StructureSection load='3rtr' size='340' side='right' caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rtr]] is a 8 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=3RTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), RBX1, RNF75, ROC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RBX1, RNF75, ROC1 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [http://www.ebi.ac.uk/pdbsum/3rtr 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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [http://pdbe.org/3rtr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [http://www.ebi.ac.uk/pdbsum/3rtr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 3rtr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
		+	*[[Cullin\|Cullin]]
		+	*[[RING box protein\|RING box protein]]
	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]		*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
Line 24:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Calabrese, M F]]		[[Category: Calabrese, M F]]
	[[Category: Duda, D M]]		[[Category: Duda, D M]]

OCA at 03:13, 25 December 2014

OCA — Thu, 25 Dec 2014 03:13:00 GMT

←Older revision		Revision as of 03:13, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTR FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RBX1, RNF75, ROC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RBX1, RNF75, ROC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [http://www.ebi.ac.uk/pdbsum/3rtr 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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [http://www.ebi.ac.uk/pdbsum/3rtr PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CUL1_HUMAN CUL1_HUMAN]] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110 (By similarity).<ref>PMID:9663463</ref> <ref>PMID:15531760</ref> <ref>PMID:15640526</ref> <ref>PMID:18644861</ref> <ref>PMID:19679664</ref> [[http://www.uniprot.org/uniprot/RBX1_HUMAN RBX1_HUMAN]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.<ref>PMID:10579999</ref> <ref>PMID:11027288</ref> <ref>PMID:16751180</ref> <ref>PMID:16678110</ref> <ref>PMID:19679664</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.,Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, Kriwacki RW, Schulman BA Nat Struct Mol Biol. 2011 Jul 17;18(8):947-9. doi: 10.1038/nsmb.2086. PMID:21765416<ref>PMID:21765416</ref>		A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.,Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, Kriwacki RW, Schulman BA Nat Struct Mol Biol. 2011 Jul 17;18(8):947-9. doi: 10.1038/nsmb.2086. PMID:21765416<ref>PMID:21765416</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>

Line 23:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Calabrese, M F.]]	+	[[Category: Calabrese, M F]]
-	[[Category: Duda, D M.]]	+	[[Category: Duda, D M]]
-	[[Category: Grace, C R.]]	+	[[Category: Grace, C R]]
-	[[Category: Kriwacki, R W.]]	+	[[Category: Kriwacki, R W]]
-	[[Category: Kurinov, I.]]	+	[[Category: Kurinov, I]]
-	[[Category: Schulman, B A.]]	+	[[Category: Schulman, B A]]
-	[[Category: Scott, D C.]]	+	[[Category: Scott, D C]]
	[[Category: Cullin]]		[[Category: Cullin]]
	[[Category: E3 ligase]]		[[Category: E3 ligase]]

OCA at 04:42, 5 June 2014

OCA — Thu, 05 Jun 2014 04:42:11 GMT

←Older revision		Revision as of 04:42, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3rtr.~~png~~\|~~left~~\|~~200px~~]]	+	==A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases==
		+	<StructureSection load='3rtr' size='340' side='right' caption='[[3rtr]], [[Resolution\|resolution]] 3.21Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTR FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RBX1, RNF75, ROC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rtr RCSB], [http://www.ebi.ac.uk/pdbsum/3rtr PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.

-	<!--	+	A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.,Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, Kriwacki RW, Schulman BA Nat Struct Mol Biol. 2011 Jul 17;18(8):947-9. doi: 10.1038/nsmb.2086. PMID:21765416<ref>PMID:21765416</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3rtr"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	-->	+
-	~~{{STRUCTURE_3rtr\| PDB=3rtr \| SCENE= }}~~	+

-	~~===A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21765416}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 21765416 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_21765416}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~3rtr~~]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021765416<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Calabrese, M F.]]		[[Category: Calabrese, M F.]]

OCA at 05:01, 24 August 2011

OCA — Wed, 24 Aug 2011 05:01:59 GMT

←Older revision		Revision as of 05:01, 24 August 2011
Line 11:		Line 11:
	===A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases===		===A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21765416}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21765416 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21765416}}

	==About this Structure==		==About this Structure==
	[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA].		[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021765416</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Calabrese, M F.]]		[[Category: Calabrese, M F.]]

OCA at 06:15, 27 July 2011

OCA — Wed, 27 Jul 2011 06:15:43 GMT

←Older revision		Revision as of 06:15, 27 July 2011
Line 1:		Line 1:
-	[[Image:3rtr.~~jpg~~\|left\|200px]]	+	[[Image:3rtr.png\|left\|200px]]

	<!--		<!--

OCA at 06:57, 20 July 2011

OCA — Wed, 20 Jul 2011 06:57:33 GMT

←Older revision		Revision as of 06:57, 20 July 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3rtr.jpg\|left\|200px]]

-	The ~~entry 3rtr~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3rtr", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3rtr\| PDB=3rtr \| SCENE= }}

-	~~Authors: Calabrese, M.F., Scott, D.C., Duda, D.M., Grace, C.R., Kurinov, I., Kriwacki, R.W., Schulman, B.~~A.	+	===A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases===

-	~~Description~~: A ~~RING~~ E3~~-substrate complex poised for ubiquitin-like protein transfer~~: ~~structural insights into cullin-RING ligases~~	+
		+	==About this Structure==
		+	[[3rtr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTR OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Calabrese, M F.]]
		+	[[Category: Duda, D M.]]
		+	[[Category: Grace, C R.]]
		+	[[Category: Kriwacki, R W.]]
		+	[[Category: Kurinov, I.]]
		+	[[Category: Schulman, B A.]]
		+	[[Category: Scott, D C.]]
		+	[[Category: Cullin]]
		+	[[Category: E3 ligase]]
		+	[[Category: Ligase]]
		+	[[Category: Nedd8]]
		+	[[Category: Ubiquitin]]
		+	[[Category: Ubl conjugation pathway]]

OCA at 18:22, 6 July 2011

OCA — Wed, 06 Jul 2011 18:22:28 GMT

←Older revision		Revision as of 18:22, 6 July 2011
Line 5:		Line 5:
	Authors: Calabrese, M.F., Scott, D.C., Duda, D.M., Grace, C.R., Kurinov, I., Kriwacki, R.W., Schulman, B.A.		Authors: Calabrese, M.F., Scott, D.C., Duda, D.M., Grace, C.R., Kurinov, I., Kriwacki, R.W., Schulman, B.A.

-	Description: E3-substrate complex	+	Description: A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases

OCA at 05:15, 18 May 2011

OCA — Wed, 18 May 2011 05:15:36 GMT

←Older revision		Revision as of 05:15, 18 May 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3rtr is ON HOLD	+	The entry 3rtr is ON HOLD until Paper Publication

	Authors: Calabrese, M.F., Scott, D.C., Duda, D.M., Grace, C.R., Kurinov, I., Kriwacki, R.W., Schulman, B.A.		Authors: Calabrese, M.F., Scott, D.C., Duda, D.M., Grace, C.R., Kurinov, I., Kriwacki, R.W., Schulman, B.A.

	Description: E3-substrate complex		Description: E3-substrate complex