4m3l: Difference between revisions
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==Crystal Structure of the coiled coil domain of MuRF1== | ==Crystal Structure of the coiled coil domain of MuRF1== | ||
<StructureSection load='4m3l' size='340' side='right' caption='[[4m3l]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4m3l' size='340' side='right'caption='[[4m3l]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4m3l]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4m3l]] is a 4 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=4M3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M3L FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=4m3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m3l OCA], [https://pdbe.org/4m3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m3l RCSB], [https://www.ebi.ac.uk/pdbsum/4m3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m3l ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TRI63_HUMAN TRI63_HUMAN] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.<ref>PMID:11927605</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Mur ligase|Mur ligase]] | *[[Mur ligase|Mur ligase]] | ||
*[[Ubiquitin protein ligase|Ubiquitin protein ligase]] | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Franke B]] | ||
[[Category: | [[Category: Mayans O]] | ||
Revision as of 13:51, 21 December 2022
Crystal Structure of the coiled coil domain of MuRF1Crystal Structure of the coiled coil domain of MuRF1
Structural highlights
FunctionTRI63_HUMAN E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.[1] Publication Abstract from PubMedMuRF1 is an E3 ubiquitin ligase central to muscle catabolism. It belongs to the TRIM protein family characterized by a tripartite fold of RING, B-box and coiled-coil (CC) motifs, followed by variable C-terminal domains. The CC motif is hypothesized to be responsible for domain organization in the fold as well as for high-order assembly into functional entities. But data on CC from this family that can clarify the structural significance of this motif are scarce. We have characterized the helical region from MuRF1 and show that, contrary to expectations, its CC domain assembles unproductively, being the B2- and COS-boxes in the fold (respectively flanking the CC) that promote a native quaternary structure. In particular, the C-terminal COS-box seemingly forms an alpha-hairpin that packs against the CC, influencing its dimerization. This shows that a C-terminal variable domain can be tightly integrated within the conserved TRIM fold to modulate its structure and function. Furthermore, data from transfected muscle show that in MuRF1 the COS-box mediates the in vivo targeting of sarcoskeletal structures and points to the pharmacological relevance of the COS domain for treating MuRF1-mediated muscle atrophy. Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1.,Franke B, Gasch A, Rodriguez D, Chami M, Khan MM, Rudolf R, Bibby J, Hanashima A, Bogomolovas J, von Castelmur E, Rigden DJ, Uson I, Labeit S, Mayans O Open Biol. 2014 Mar 26;4:130172. doi: 10.1098/rsob.130172. PMID:24671946[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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