2ru6 - Revision history

OCA at 20:52, 12 April 2023

OCA — Wed, 12 Apr 2023 20:52:55 GMT

←Older revision		Revision as of 20:52, 12 April 2023
Line 1:		Line 1:

	==The pure alternative state of ubiquitin==		==The pure alternative state of ubiquitin==
-	<StructureSection load='2ru6' size='340' side='right'caption='[[2ru6~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2ru6' size='340' side='right'caption='[[2ru6]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rsu\|2rsu]]</div></td></tr>~~	+	</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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [https://pdbe.org/2ru6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ru6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru6 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [https://pdbe.org/2ru6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ru6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baxter, N]]	+	[[Category: Baxter N]]
-	[[Category: Kameda, T]]	+	[[Category: Kameda T]]
-	[[Category: Kato, K]]	+	[[Category: Kato K]]
-	[[Category: Kitahara, R]]	+	[[Category: Kitahara R]]
-	[[Category: Kitazawa, S]]	+	[[Category: Kitazawa S]]
-	[[Category: Kumo, A]]	+	[[Category: Kumo A]]
-	[[Category: Utsumi, M]]	+	[[Category: Utsumi M]]
-	[[Category: Williamson~~, M P]]~~	+	[[Category: Williamson MP]]
-	~~[[Category: Alternatively folded state]]~~	+
-	~~[[Category: High-pressure nmr]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Q41n variant]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 10:36, 7 July 2021

OCA — Wed, 07 Jul 2021 10:36:49 GMT

←Older revision		Revision as of 10:36, 7 July 2021
Line 1:		Line 1:

	==The pure alternative state of ubiquitin==		==The pure alternative state of ubiquitin==
-	<StructureSection load='2ru6' size='340' side='right' caption='[[2ru6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2ru6' size='340' side='right'caption='[[2ru6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rsu\|2rsu]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([~~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">UBC ([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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [~~http~~://pdbe.org/2ru6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ru6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru6 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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [https://pdbe.org/2ru6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ru6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</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==
-	*[[~~Ubiquitin~~\|~~Ubiquitin~~]]	+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Baxter, N]]		[[Category: Baxter, N]]
	[[Category: Kameda, T]]		[[Category: Kameda, T]]

OCA at 14:01, 4 August 2016

OCA — Thu, 04 Aug 2016 14:01:39 GMT

←Older revision		Revision as of 14:01, 4 August 2016
Line 1:		Line 1:
		+
	==The pure alternative state of ubiquitin==		==The pure alternative state of ubiquitin==
	<StructureSection load='2ru6' size='340' side='right' caption='[[2ru6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2ru6' size='340' side='right' caption='[[2ru6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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">UBC ([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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://pdbe.org/2ru6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru6 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 2ru6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 15:23, 24 December 2014

OCA — Wed, 24 Dec 2014 15:23:19 GMT

←Older revision		Revision as of 15:23, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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">UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme.,Kitazawa S, Kameda T, Kumo A, Yagi-Utsumi M, Baxter NJ, Kato K, Williamson MP, Kitahara R Biochemistry. 2014 Jan 28;53(3):447-9. doi: 10.1021/bi401617n. Epub 2014 Jan 10. PMID:24401037<ref>PMID:24401037</ref>		Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme.,Kitazawa S, Kameda T, Kumo A, Yagi-Utsumi M, Baxter NJ, Kato K, Williamson MP, Kitahara R Biochemistry. 2014 Jan 28;53(3):447-9. doi: 10.1021/bi401617n. Epub 2014 Jan 10. PMID:24401037<ref>PMID:24401037</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>
		+
		+	==See Also==
		+	*[[Ubiquitin\|Ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
Line 20:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Baxter, N.]]	+	[[Category: Baxter, N]]
-	[[Category: Kameda, T.]]	+	[[Category: Kameda, T]]
-	[[Category: Kato, K.]]	+	[[Category: Kato, K]]
-	[[Category: Kitahara, R.]]	+	[[Category: Kitahara, R]]
-	[[Category: Kitazawa, S.]]	+	[[Category: Kitazawa, S]]
-	[[Category: Kumo, A.]]	+	[[Category: Kumo, A]]
-	[[Category: Utsumi, M.]]	+	[[Category: Utsumi, M]]
-	[[Category: Williamson, M P.]]	+	[[Category: Williamson, M P]]
	[[Category: Alternatively folded state]]		[[Category: Alternatively folded state]]
	[[Category: High-pressure nmr]]		[[Category: High-pressure nmr]]

OCA at 12:54, 18 May 2014

OCA — Sun, 18 May 2014 12:54:06 GMT

←Older revision		Revision as of 12:54, 18 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2ru6~~\| ~~PDB~~=2ru6 \| ~~SCENE~~= }}	+	==The pure alternative state of ubiquitin==
-	===~~The pure alternative state of ubiquitin~~===	+	<StructureSection load='2ru6' size='340' side='right' caption='[[2ru6]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_24401037}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RU6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rsu\|2rsu]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We present the nuclear Overhauser effect-based structure determination of the Q41N variant of ubiquitin at 2500 bar, where the alternatively folded N2 state is 97% populated. This allows us to characterize the structure of the "pure" N2 state of ubiquitin. The N2 state shows a substantial change in the orientation of strand beta5 compared to that of the normal folded N1 state, which matches the changes seen upon binding of ubiquitin to ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is therefore best explained by conformational selection rather than induced-fit motion.

-	~~==Function==~~	+	Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme.,Kitazawa S, Kameda T, Kumo A, Yagi-Utsumi M, Baxter NJ, Kato K, Williamson MP, Kitahara R Biochemistry. 2014 Jan 28;53(3):447-9. doi: 10.1021/bi401617n. Epub 2014 Jan 10. PMID:24401037<ref>PMID:24401037</ref>
-	~~[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]]~~ Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the ~~initiator Met~~ of the ~~ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached~~ to ~~a target protein, have different functions depending on~~ the ~~Lys residue of the ubiquitin that is linked: Lys~~-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. ~~Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins~~, ~~however~~, ~~in rare cases~~, ~~conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored~~-~~polyubiquitin)~~, ~~it also has distinct roles~~, ~~such as in activation of protein kinases~~, ~~and in signaling~~.~~<ref>~~PMID:~~16543144</ref>~~ <ref>PMID:~~19754430~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2ru6]] is~~ a ~~1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=2RU6 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024401037</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Baxter, N.]]		[[Category: Baxter, N.]]
	[[Category: Kameda, T.]]		[[Category: Kameda, T.]]
Line 22:		Line 31:
	[[Category: High-pressure nmr]]		[[Category: High-pressure nmr]]
	[[Category: Protein binding]]		[[Category: Protein binding]]
		+	[[Category: Q41n variant]]
	[[Category: Ubiquitin]]		[[Category: Ubiquitin]]

OCA at 05:03, 13 February 2014

OCA — Thu, 13 Feb 2014 05:03:21 GMT

←Older revision		Revision as of 05:03, 13 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_2ru6\| PDB=2ru6 \| SCENE= }}
		+	===The pure alternative state of ubiquitin===
		+	{{ABSTRACT_PUBMED_24401037}}

-	~~The entry 2ru6~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>

-	~~Authors~~: ~~Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K~~.~~, Williamson, M~~.P.~~, Kitahara, R~~.	+	==About this Structure==
		+	[[2ru6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA].

-	~~Description~~: ~~The pure alternative~~ state ~~of ubiquitin~~	+	==Reference==
		+	<ref group="xtra">PMID:024401037</ref><references group="xtra"/><references/>
		+	[[Category: Baxter, N.]]
		+	[[Category: Kameda, T.]]
		+	[[Category: Kato, K.]]
		+	[[Category: Kitahara, R.]]
		+	[[Category: Kitazawa, S.]]
		+	[[Category: Kumo, A.]]
		+	[[Category: Utsumi, M.]]
		+	[[Category: Williamson, M P.]]
		+	[[Category: Alternatively folded state]]
		+	[[Category: High-pressure nmr]]
		+	[[Category: Protein binding]]
		+	[[Category: Ubiquitin]]

OCA at 07:20, 15 January 2014

OCA — Wed, 15 Jan 2014 07:20:14 GMT

←Older revision		Revision as of 07:20, 15 January 2014
Line 5:		Line 5:
	Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.		Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.

-	Description: ~~the~~ pure alternative state of ubiquitin	+	Description: The pure alternative state of ubiquitin

OCA at 08:36, 8 January 2014

OCA — Wed, 08 Jan 2014 08:36:34 GMT

←Older revision		Revision as of 08:36, 8 January 2014
Line 5:		Line 5:
	Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.		Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.

-	Description: ~~The~~ pure alternative state of ubiquitin	+	Description: the pure alternative state of ubiquitin

OCA at 09:01, 25 December 2013

OCA — Wed, 25 Dec 2013 09:01:33 GMT

←Older revision		Revision as of 09:01, 25 December 2013
Line 5:		Line 5:
	Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.		Authors: Kitazawa, S., Kameda, T., Kumo, A., Utsumi, M., Baxter, N., Kato, K., Williamson, M.P., Kitahara, R.

-	Description: ~~the~~ pure alternative state of ubiquitin	+	Description: The pure alternative state of ubiquitin

OCA: Protected "2ru6" [edit=sysop:move=sysop]

OCA — Wed, 11 Dec 2013 12:40:54 GMT

Protected "2ru6" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:40, 11 December 2013