2msg - Revision history

OCA at 06:09, 15 May 2024

2024-05-15T06:09:48Z

← Older revision		Revision as of 06:09, 15 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
	</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [https://pdbe.org/2msg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [https://www.ebi.ac.uk/pdbsum/2msg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [https://pdbe.org/2msg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [https://www.ebi.ac.uk/pdbsum/2msg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 09:44, 14 June 2023

2023-06-14T09:44:13Z

← Older revision		Revision as of 09:44, 14 June 2023
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	==Solid-state NMR structure of ubiquitin==		==Solid-state NMR structure of ubiquitin==
	<StructureSection load='2msg' size='340' side='right'caption='[[2msg~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>		<StructureSection load='2msg' size='340' side='right'caption='[[2msg]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSG 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;'>[[3ons\|3ons]], [[1d3z\|1d3z]]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [https://pdbe.org/2msg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [https://www.ebi.ac.uk/pdbsum/2msg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg 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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [https://pdbe.org/2msg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [https://www.ebi.ac.uk/pdbsum/2msg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg 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 ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Becker, S]]		[[Category: Becker S]]
	[[Category: Fasshuber, H]]		[[Category: Fasshuber H]]
	[[Category: Giller, K]]		[[Category: Giller K]]
	[[Category: Habenstein, B]]		[[Category: Habenstein B]]
	[[Category: Lakomek, N]]		[[Category: Lakomek N]]
	[[Category: Lange, A]]		[[Category: Lange A]]
	[[Category: Loquet, A]]		[[Category: Loquet A]]
	[[Category: Shi, C]]		[[Category: Shi C]]
	[[Category: Wolff, S]]		[[Category: Wolff S]]
	~~[[Category: Signaling protein]]~~
	~~[[Category: Ubiquitin fold~~]]

OCA at 10:09, 22 June 2022

2022-06-22T10:09:40Z

← Older revision		Revision as of 10:09, 22 June 2022
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	<StructureSection load='2msg' size='340' side='right'caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2msg' size='340' side='right'caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</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;'>[[3ons\|3ons]], [[1d3z\|1d3z]]</div></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [~~http~~://pdbe.org/2msg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2msg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg 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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [https://pdbe.org/2msg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [https://www.ebi.ac.uk/pdbsum/2msg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg 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 ==

OCA at 10:43, 16 September 2020

2020-09-16T10:43:13Z

← Older revision		Revision as of 10:43, 16 September 2020
Line 1:		Line 1:

	==Solid-state NMR structure of ubiquitin==		==Solid-state NMR structure of ubiquitin==
	<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2msg' size='340' side='right'caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://pdbe.org/2msg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://pdbe.org/2msg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Becker, S]]		[[Category: Becker, S]]
	[[Category: Fasshuber, H]]		[[Category: Fasshuber, H]]

OCA at 07:56, 12 December 2018

2018-12-12T07:56:24Z

← Older revision		Revision as of 07:56, 12 December 2018
Line 3:		Line 3:
	<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2msg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] 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=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://pdbe.org/2msg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://pdbe.org/2msg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg ProSAT]</span></td></tr>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Becker, S]]		[[Category: Becker, S]]
	[[Category: Fasshuber, H]]		[[Category: Fasshuber, H]]

OCA at 17:35, 9 March 2017

2017-03-09T17:35:55Z

← Older revision		Revision as of 17:35, 9 March 2017
Line 1:		Line 1:

	==Solid-state NMR structure of ubiquitin==		==Solid-state NMR structure of ubiquitin==
	<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2msg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2msg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg 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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://pdbe.org/2msg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2msg 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 2msg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:00, 18 February 2015

2015-02-18T13:00:21Z

← Older revision		Revision as of 13:00, 18 February 2015
Line 1:		Line 1:
	'''~~Unreleased~~ structure'''		==Solid-state NMR structure of ubiquitin==
			<StructureSection load='2msg' size='340' side='right' caption='[[2msg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2msg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSG FirstGlance]. <br>
			</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ons\|3ons]], [[1d3z\|1d3z]]</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=2msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2msg RCSB], [http://www.ebi.ac.uk/pdbsum/2msg 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>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			By applying [1-13 C]- and [2-13 C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 A to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop regions beta1-beta2 but also for beta-strands beta1, beta2, beta3 and beta5 as well as for the loop connecting alpha1 and beta3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales. This article is protected by copyright. All rights reserved.

	~~The entry 2msg is ON HOLD until Paper Publication~~		Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.,Fasshuber HK, Lakomek NA, Habenstein B, Loquet A, Shi C, Giller K, Wolff S, Becker S, Lange A Protein Sci. 2015 Feb 2. doi: 10.1002/pro.2654. PMID:25644665<ref>PMID:25644665</ref>

	~~Authors: Lakomek~~, N.~~, Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff,~~ S.~~, Becker, S., Fasshuber, H., Lange, A~~.		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD~~		== References ==
	~~[[Category: Unreleased Structures]]~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Becker, S]]		[[Category: Becker, S]]
			[[Category: Fasshuber, H]]
			[[Category: Giller, K]]
			[[Category: Habenstein, B]]
			[[Category: Lakomek, N]]
	[[Category: Lange, A]]		[[Category: Lange, A]]
	[[Category: ~~Habenstein~~, B]]		[[Category: Loquet, A]]
	[[Category: Shi, C]]		[[Category: Shi, C]]
	~~[[Category: Loquet, A]]~~
	~~[[Category: Fasshuber, H]]~~
	~~[[Category: Lakomek, N]]~~
	[[Category: Wolff, S]]		[[Category: Wolff, S]]
	[[Category: ~~Giller, K~~]]		[[Category: Signaling protein]]
			[[Category: Ubiquitin fold]]

OCA at 12:20, 24 December 2014

2014-12-24T12:20:39Z

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	Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD		Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD
			[[Category: Unreleased Structures]]
			[[Category: Becker, S]]
			[[Category: Lange, A]]
			[[Category: Habenstein, B]]
			[[Category: Shi, C]]
			[[Category: Loquet, A]]
			[[Category: Fasshuber, H]]
			[[Category: Lakomek, N]]
			[[Category: Wolff, S]]
			[[Category: Giller, K]]

OCA at 06:05, 27 August 2014

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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 2msg is ON HOLD		The entry 2msg is ON HOLD until Paper Publication

	Authors: Lakomek, N., Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff, S., Becker, S.		Authors: Lakomek, N., Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff, S., Becker, S., Fasshuber, H., Lange, A.

	Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD		Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD

OCA at 13:52, 20 August 2014

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	Authors: Lakomek, N., Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff, S., Becker, S.		Authors: Lakomek, N., Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff, S., Becker, S.

	Description: 13C,15N solid-state NMR chemical shift assignments for ~~microcrystallized Ubiquitinin~~ MPD		Description: 13C,15N solid-state NMR chemical shift assignments for microcrystalline Ubiquitin in MPD