2mor - Revision history

OCA at 07:01, 1 May 2024

2024-05-01T07:01:33Z

← Older revision		Revision as of 07:01, 1 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOR 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [https://pdbe.org/2mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [https://www.ebi.ac.uk/pdbsum/2mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [https://pdbe.org/2mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [https://www.ebi.ac.uk/pdbsum/2mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor 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;">~~
	~~== Publication Abstract from PubMed ==~~
	Residual dipolar couplings (RDCs) are parameters measured in nuclear magnetic resonance spectroscopy that can provide exquisitely detailed information about the structure and dynamics of biological macromolecules. We describe here a method of using RDCs for the structural and dynamical refinement of proteins that is based on the observation that the RDC between two atomic nuclei depends directly on the angle vartheta between the internuclear vector and the external magnetic field. For every pair of nuclei for which an RDC is available experimentally, we introduce a structural restraint to minimize the deviation from the value of the angle vartheta derived from the measured RDC and that calculated in the refinement protocol. As each restraint involves only the calculation of the angle vartheta of the corresponding internuclear vector, the method does not require the definition of an overall alignment tensor to describe the preferred orientation of the protein with respect to the alignment medium. Application to the case of ubiquitin demonstrates that this method enables an accurate refinement of the structure and dynamics of this protein to be obtained.

	A Tensor-Free Method for the Structural and Dynamical Refinement of Proteins using Residual Dipolar Couplings.,Camilloni C, Vendruscolo M J Phys Chem B. 2014 Jun 4. PMID:24824082<ref>PMID:24824082</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2mor" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:02, 8 March 2023

2023-03-08T08:02:50Z

← Older revision		Revision as of 08:02, 8 March 2023
Line 1:		Line 1:

	==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==		==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==
	<StructureSection load='2mor' size='340' side='right'caption='[[2mor~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>		<StructureSection load='2mor' size='340' side='right'caption='[[2mor]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOR 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;'>[[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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [https://pdbe.org/2mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [https://www.ebi.ac.uk/pdbsum/2mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [https://pdbe.org/2mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [https://www.ebi.ac.uk/pdbsum/2mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor 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 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Camilloni, C]]		[[Category: Camilloni C]]
	[[Category: Vendruscolo, M]]		[[Category: Vendruscolo M]]
	~~[[Category: Signaling protein]]~~
	~~[[Category: Ubiquitin~~]]

OCA at 15:18, 2 June 2021

2021-06-02T15:18:15Z

← Older revision		Revision as of 15:18, 2 June 2021
Line 1:		Line 1:

	==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==		==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==
	<StructureSection load='2mor' size='340' side='right' caption='[[2mor]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='2mor' size='340' side='right'caption='[[2mor]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[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;'>[[1d3z\|1d3z]]</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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [~~http~~://pdbe.org/2mor PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2mor PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [https://pdbe.org/2mor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [https://www.ebi.ac.uk/pdbsum/2mor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor 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 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Camilloni, C]]		[[Category: Camilloni, C]]
	[[Category: Vendruscolo, M]]		[[Category: Vendruscolo, M]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Ubiquitin]]		[[Category: Ubiquitin]]

OCA at 17:02, 15 August 2018

2018-08-15T17:02:20Z

← Older revision		Revision as of 17:02, 15 August 2018
Line 1:		Line 1:

	==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==		==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==
	<StructureSection load='2mor' size='340' side='right' caption='[[2mor]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='2mor' size='340' side='right' caption='[[2mor]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mor]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] 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=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://pdbe.org/2mor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor PDBsum]</span></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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://pdbe.org/2mor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mor ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Camilloni, C]]		[[Category: Camilloni, C]]
	[[Category: Vendruscolo, M]]		[[Category: Vendruscolo, M]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Ubiquitin]]		[[Category: Ubiquitin]]

OCA at 07:41, 10 September 2015

2015-09-10T07:41:04Z

← Older revision		Revision as of 07:41, 10 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[2mor]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://pdbe.org/2mor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	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 2mor" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:28, 24 December 2014

2014-12-24T20:28:58Z

← Older revision		Revision as of 20:28, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mor]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mor]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOR FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d3z\|1d3z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d3z\|1d3z]]</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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor 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=2mor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mor RCSB], [http://www.ebi.ac.uk/pdbsum/2mor 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 18:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Camilloni, C.]]		[[Category: Camilloni, C]]
	[[Category: Vendruscolo, M.]]		[[Category: Vendruscolo, M]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Ubiquitin]]		[[Category: Ubiquitin]]

OCA at 06:22, 25 June 2014

2014-06-25T06:22:59Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings==
-The entry 2mor is ON HOLD  until Paper Publication
+A Tensor-Free Method for the Structural and Dynamical Refinement of Proteins using Residual Dipolar Couplings.,Camilloni C, Vendruscolo M J Phys Chem B. 2014 Jun 4. PMID:24824082<ref>PMID:24824082</ref>
-Authors: Camilloni, C., Vendruscolo, M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings
+== References ==

OCA at 06:59, 14 May 2014

2014-05-14T06:59:59Z

← Older revision		Revision as of 06:59, 14 May 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Camilloni, C., Vendruscolo, M.		Authors: Camilloni, C., Vendruscolo, M.

	Description: ~~Validation~~ of ~~Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase~~		Description: A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings

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

2014-05-07T07:12:11Z

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

← Older revision	Revision as of 07:12, 7 May 2014
(No difference)

OCA: New page: '''Unreleased structure''' The entry 2mor is ON HOLD Authors: Camilloni, C., Vendruscolo, M. Description: Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a...

2014-05-07T07:12:10Z

New page: '''Unreleased structure''' The entry 2mor is ON HOLD Authors: Camilloni, C., Vendruscolo, M. Description: Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a...

New page

'''Unreleased structure'''

The entry 2mor is ON HOLD

Authors: Camilloni, C., Vendruscolo, M.

Description: Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase