2kox: Difference between revisions

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-{{Large structure}}
-[[Image:2kox.png|left|200px]]
-<!--
+==NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin==
-The line below this paragraph, containing "STRUCTURE_2kox", creates the "Structure Box" on the page.
+<StructureSection load='2kox' size='340' side='right'caption='[[2kox]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_2kox|  PDB=2kox  |  SCENE=  }}
+</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>
-===NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin===
+==See Also==
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_21634390}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 21634390 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_21634390}}
-==About this Structure==
-[[2kox]] is a 1 chain structure with sequence from [http://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].
-==Reference==
-<ref group="xtra">PMID:021634390</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Becker, S.]]
+[[Category: Large Structures]]
-[[Category: Fenwick, R B.]]
+[[Category: Becker S]]
-[[Category: Griesinger, C.]]
+[[Category: Fenwick RB]]
-[[Category: Lakomek, N A.]]
+[[Category: Griesinger C]]
-[[Category: Lee, D.]]
+[[Category: Lakomek NA]]
-[[Category: Milovanovic, D.]]
+[[Category: Lee D]]
-[[Category: Richter, B.]]
+[[Category: Milovanovic D]]
-[[Category: Salvatella, X.]]
+[[Category: Richter B]]
-[[Category: Walter, K F.A.]]
+[[Category: Salvatella X]]
-[[Category: Isopeptide bond]]
+[[Category: Walter KFA]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Residual dipolar coupling]]
-[[Category: Signaling protein]]
-[[Category: Simulated annealing]]
-[[Category: Ubiquitin]]