9pl1

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Current revision (05:52, 6 August 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9pl1 is ON HOLD
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==Structure of metastable folding intermediate of V17A/V26A ubiquitin derived from pressure-jump NMR data==
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<StructureSection load='9pl1' size='340' side='right'caption='[[9pl1]]' scene=''>
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Authors: Masoumzadeh, E., Courtney, J.M., Bax, A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9pl1]] 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=9PL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PL1 FirstGlance]. <br>
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Description: Structure of metastable folding intermediate of V17A/V26A ubiquitin derived from pressure-jump NMR data
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9pl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pl1 OCA], [https://pdbe.org/9pl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pl1 RCSB], [https://www.ebi.ac.uk/pdbsum/9pl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pl1 ProSAT]</span></td></tr>
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[[Category: Courtney, J.M]]
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</table>
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[[Category: Bax, A]]
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== Function ==
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[[Category: Masoumzadeh, E]]
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[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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Bax A]]
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[[Category: Courtney JM]]
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[[Category: Masoumzadeh E]]

Current revision

Structure of metastable folding intermediate of V17A/V26A ubiquitin derived from pressure-jump NMR data

PDB ID 9pl1

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