3axc

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[[Image:3axc.png|left|200px]]
 
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==Crystal structure of linear diubiquitin==
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The line below this paragraph, containing "STRUCTURE_3axc", creates the "Structure Box" on the page.
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<StructureSection load='3axc' size='340' side='right'caption='[[3axc]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3axc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AXC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3axc| PDB=3axc | SCENE= }}
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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=3axc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axc OCA], [https://pdbe.org/3axc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3axc RCSB], [https://www.ebi.ac.uk/pdbsum/3axc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3axc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RS27A_HUMAN RS27A_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 S27a is a component of the 40S subunit of the ribosome.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Post-translational modifications involving ubiquitin regulate a wide range of biological processes including protein degradation, responses to DNA damage and immune signalling. Ubiquitin polymerizes into chains which may contain eight different linkage types; the ubiquitin C-terminal glycine can link to one of the seven lysine residues or the N-terminal amino group of methionine in the distal ubiquitin molecule. The latter head-to-tail linkage type, referred to as a linear ubiquitin chain, is involved in NF-kappaB activation through specific interactions with NF-kappaB essential modulator (NEMO). Here, a crystal structure of linear diubiquitin at a resolution of 2.2 A is reported. Although the two ubiquitin moieties do not interact with each other directly, the overall structure adopts a compact but not completely closed conformation with a few intermoiety contacts. This structure differs from the previously reported extended conformation, which resembles Lys63-linked diubiquitin, suggesting that the linear polyubiquitin chain is intrinsically flexible and can adopt multiple conformations.
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===Crystal structure of linear diubiquitin===
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Structure of a compact conformation of linear diubiquitin.,Rohaim A, Kawasaki M, Kato R, Dikic I, Wakatsuki S Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):102-8. Epub 2012 Jan 13. PMID:22281738<ref>PMID:22281738</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3axc" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22281738}}, adds the Publication Abstract to the page
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22281738 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22281738}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3axc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXC OCA].
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==Reference==
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<ref group="xtra">PMID:022281738</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dikic, I.]]
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[[Category: Large Structures]]
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[[Category: Kato, R.]]
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[[Category: Dikic I]]
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[[Category: Kawasaki, M.]]
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[[Category: Kato R]]
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[[Category: Rohaim, A.]]
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[[Category: Kawasaki M]]
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[[Category: Wakatsuki, S.]]
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[[Category: Rohaim A]]
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[[Category: Nf kappa b signaling]]
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[[Category: Wakatsuki S]]
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[[Category: Signaling protein]]
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Current revision

Crystal structure of linear diubiquitin

PDB ID 3axc

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