2kox: Difference between revisions

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==NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin==
==NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin==
<StructureSection load='2kox' size='340' side='right'caption='[[2kox]], [[NMR_Ensembles_of_Models | 640 NMR models]]' scene=''>
<StructureSection load='2kox' size='340' side='right'caption='[[2kox]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kox]] 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=2KOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KOX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kox]] 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=2KOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KOX 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;'>[[2k39|2k39]], [[1d3z|1d3z]], [[2nr2|2nr2]], [[1ubq|1ubq]]</div></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=2kox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kox OCA], [https://pdbe.org/2kox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kox RCSB], [https://www.ebi.ac.uk/pdbsum/2kox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kox 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=2kox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kox OCA], [https://pdbe.org/2kox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kox RCSB], [https://www.ebi.ac.uk/pdbsum/2kox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kox ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL40_HUMAN RL40_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>  Ribosomal protein L40 is a component of the 60S subunit of the ribosome.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
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<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: Fenwick, R B]]
[[Category: Fenwick RB]]
[[Category: Griesinger, C]]
[[Category: Griesinger C]]
[[Category: Lakomek, N A]]
[[Category: Lakomek NA]]
[[Category: Lee, D]]
[[Category: Lee D]]
[[Category: Milovanovic, D]]
[[Category: Milovanovic D]]
[[Category: Richter, B]]
[[Category: Richter B]]
[[Category: Salvatella, X]]
[[Category: Salvatella X]]
[[Category: Walter, K F.A]]
[[Category: Walter KFA]]
[[Category: Isopeptide bond]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Residual dipolar coupling]]
[[Category: Signaling protein]]
[[Category: Simulated annealing]]
[[Category: Ubiquitin]]

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