3axc: Difference between revisions
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[[ | ==Crystal structure of linear diubiquitin== | ||
<StructureSection load='3axc' size='340' side='right' caption='[[3axc]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXC FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPS27A, UBA80, UBCEP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3axc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3axc RCSB], [http://www.ebi.ac.uk/pdbsum/3axc PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Dikic, I.]] | [[Category: Dikic, I.]] | ||