3zlz - Revision history

OCA at 11:05, 20 December 2023

OCA — Wed, 20 Dec 2023 11:05:43 GMT

←Older revision		Revision as of 11:05, 20 December 2023
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	<StructureSection load='3zlz' size='340' side='right'caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3zlz' size='340' side='right'caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zlz]] is a 2 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=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZLZ 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]] 2.9Å</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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [https://pdbe.org/3zlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [https://www.ebi.ac.uk/pdbsum/3zlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlz 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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [https://pdbe.org/3zlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [https://www.ebi.ac.uk/pdbsum/3zlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/UBB_HUMAN UBB_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/UBB_HUMAN UBB_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 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Freund~~, S M.V~~]]	+	[[Category: Freund SMV]]
-	[[Category: Hospenthal~~, M K~~]]	+	[[Category: Hospenthal MK]]
-	[[Category: Komander, D]]	+	[[Category: Komander D]]
-	~~[[Category: Atypical chain type]]~~	+
-	~~[[Category: Bacterial effector]]~~	+
-	~~[[Category: Deubiquitinase]]~~	+
-	~~[[Category: Nlel]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 07:00, 18 August 2022

OCA — Thu, 18 Aug 2022 07:00:07 GMT

←Older revision		Revision as of 07:00, 18 August 2022
Line 3:		Line 3:
	<StructureSection load='3zlz' size='340' side='right'caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3zlz' size='340' side='right'caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zlz]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zlz]] is a 2 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=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZLZ 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='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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [~~http~~://pdbe.org/3zlz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3zlz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlz 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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [https://pdbe.org/3zlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [https://www.ebi.ac.uk/pdbsum/3zlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/UBB_HUMAN UBB_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/UBB_HUMAN UBB_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 20:		Line 20:

	==See Also==		==See Also==
-	*[[~~Ubiquitin~~\|~~Ubiquitin~~]]	+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:34, 7 August 2019

OCA — Wed, 07 Aug 2019 06:34:21 GMT

←Older revision		Revision as of 06:34, 7 August 2019
Line 1:		Line 1:

	==Lys6-linked tri-ubiquitin==		==Lys6-linked tri-ubiquitin==
-	<StructureSection load='3zlz' size='340' side='right' caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='3zlz' size='340' side='right'caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3zlz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[3zlz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 3zlz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3zlz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin\|Ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Freund, S M.V]]		[[Category: Freund, S M.V]]
	[[Category: Hospenthal, M K]]		[[Category: Hospenthal, M K]]

OCA at 11:52, 6 November 2017

OCA — Mon, 06 Nov 2017 11:52:37 GMT

←Older revision		Revision as of 11:52, 6 November 2017
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 3zlz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3zlz" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Ubiquitin\|Ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:27, 4 August 2016

OCA — Thu, 04 Aug 2016 08:27:47 GMT

←Older revision		Revision as of 08:27, 4 August 2016
Line 1:		Line 1:
		+
	==Lys6-linked tri-ubiquitin==		==Lys6-linked tri-ubiquitin==
	<StructureSection load='3zlz' size='340' side='right' caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3zlz' size='340' side='right' caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zlz]] is a 2 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=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zlz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLZ 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='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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [http://www.ebi.ac.uk/pdbsum/3zlz 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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [http://pdbe.org/3zlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [http://www.ebi.ac.uk/pdbsum/3zlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 3zlz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Freund, S M.V]]		[[Category: Freund, S M.V]]
	[[Category: Hospenthal, M K]]		[[Category: Hospenthal, M K]]

OCA at 07:40, 24 December 2014

OCA — Wed, 24 Dec 2014 07:40:13 GMT

←Older revision		Revision as of 07:40, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3zlz\| PDB~~=3zlz \| ~~SCENE~~= }}	+	==Lys6-linked tri-ubiquitin==
-	===~~Lys6~~-~~linked tri~~-~~ubiquitin~~===	+	<StructureSection load='3zlz' size='340' side='right' caption='[[3zlz]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23563141}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3zlz]] is a 2 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=3ZLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLZ FirstGlance]. <br>
-	==Function==	+	</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='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=3zlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zlz RCSB], [http://www.ebi.ac.uk/pdbsum/3zlz PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_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>		[[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_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;">
		+	== Publication Abstract from PubMed ==
		+	Ubiquitin (Ub) chains regulate many cellular processes, but several chain types including Lys6 linkages have remained unstudied. Here we analyze the bacterial effector E3 ligase NleL (non-Lee-encoded effector ligase) from enterohemorrhagic Escherichia coli (EHEC) O157:H7, which assembles Lys6- and Lys48-linked Ub polymers. Using linkage-specific human deubiquitinases (DUBs) we show that NleL generates heterotypic Ub chains, and branched chains are efficiently hydrolyzed by DUBs. USP family DUBs cleave Lys6-linked polymers exclusively from the distal end, whereas a DUB with preference for Lys6 can cleave Lys6-linked polymers at any position in the chain. We used NleL to generate large quantities of Lys6-linked polyUb. Crystallographic and NMR spectroscopy analyses revealed that an asymmetric interface between Ile44 and Ile36 hydrophobic patches of neighboring Ub moieties is propagated in longer Lys6-linked Ub chains. Interactions via the Ile36 patch can displace Leu8 from the Ile44 patch, leading to marked structural perturbations of Ub.
		+
		+	Assembly, analysis and architecture of atypical ubiquitin chains.,Hospenthal MK, Freund SM, Komander D Nat Struct Mol Biol. 2013 Apr 7. doi: 10.1038/nsmb.2547. PMID:23563141<ref>PMID:23563141</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3zlz]] is~~ a ~~2 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=3ZLZ OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023563141</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Ubiquitin\|Ubiquitin]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Freund, S M.V.]]	+	[[Category: Freund, S M.V]]
-	[[Category: Hospenthal, M K.]]	+	[[Category: Hospenthal, M K]]
-	[[Category: Komander, D.]]	+	[[Category: Komander, D]]
	[[Category: Atypical chain type]]		[[Category: Atypical chain type]]
	[[Category: Bacterial effector]]		[[Category: Bacterial effector]]

OCA at 06:31, 20 June 2013

OCA — Thu, 20 Jun 2013 06:31:25 GMT

←Older revision		Revision as of 06:31, 20 June 2013
Line 10:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023563141</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Freund, S M.V.]]		[[Category: Freund, S M.V.]]

OCA at 19:12, 17 April 2013

OCA — Wed, 17 Apr 2013 19:12:57 GMT

←Older revision		Revision as of 19:12, 17 April 2013
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	{{STRUCTURE_3zlz\| PDB=3zlz \| SCENE= }}		{{STRUCTURE_3zlz\| PDB=3zlz \| SCENE= }}
	===Lys6-linked tri-ubiquitin===		===Lys6-linked tri-ubiquitin===
		+	{{ABSTRACT_PUBMED_23563141}}

	==Function==		==Function==

OCA at 22:38, 10 April 2013

OCA — Wed, 10 Apr 2013 22:38:54 GMT

←Older revision		Revision as of 22:38, 10 April 2013
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-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3zlz\| PDB=3zlz \| SCENE= }}
		+	===Lys6-linked tri-ubiquitin===

-	~~The entry 3zlz~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_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~~: ~~Hospenthal, M~~.K.~~, Freund, S~~.M.V.~~, Komander, D~~.	+	==About this Structure==
		+	[[3zlz]] is a 2 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=3ZLZ OCA].

-	~~Description~~: ~~Lys6-linked tri-ubiquitin~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Freund, S M.V.]]
		+	[[Category: Hospenthal, M K.]]
		+	[[Category: Komander, D.]]
		+	[[Category: Atypical chain type]]
		+	[[Category: Bacterial effector]]
		+	[[Category: Deubiquitinase]]
		+	[[Category: Nlel]]
		+	[[Category: Signaling protein]]

OCA at 14:06, 27 February 2013

OCA — Wed, 27 Feb 2013 14:06:28 GMT

←Older revision		Revision as of 14:06, 27 February 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Hospenthal, M.K., Freund, S.M.V., Komander, D.		Authors: Hospenthal, M.K., Freund, S.M.V., Komander, D.

	Description: Lys6-linked tri-ubiquitin		Description: Lys6-linked tri-ubiquitin