@article{Stevens2019-07-12Explo-46660,
  year={2019},
  doi={10.1016/j.jmb.2019.05.025},
  title={Exploration of the TRIM Fold of MuRF1 Using EPR Reveals a Canonical Antiparallel Structure and Extended COS-Box},
  number={15},
  volume={431},
  issn={0022-2836},
  journal={Journal of molecular biology},
  pages={2900--2909},
  author={Stevens, Michael and Franke, Barbara and Skorupka, Katarzyna A. and Cafiso, David  S. and Pornillos, Owen and Mayans, Olga and Norman, David G.}
}

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    <dc:contributor>Pornillos, Owen</dc:contributor>
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    <dc:creator>Franke, Barbara</dc:creator>
    <dc:language>eng</dc:language>
    <dc:contributor>Franke, Barbara</dc:contributor>
    <dc:creator>Norman, David G.</dc:creator>
    <dc:creator>Cafiso, David  S.</dc:creator>
    <dc:contributor>Stevens, Michael</dc:contributor>
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    <dc:creator>Pornillos, Owen</dc:creator>
    <dc:contributor>Norman, David G.</dc:contributor>
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    <dcterms:abstract xml:lang="eng">MuRF1 (TRIM63) is a RING-type E3 ubiquitin ligase with a predicted tripartite TRIM fold. TRIM proteins rely upon the correct placement of an N-terminal RING domain, with respect to C-terminal, specific substrate-binding domains. The TRIM domain organization is orchestrated by a central helical domain that forms an antiparallel coiled-coil motif and mediates the dimerization of the fold. MuRF1 has a reduced TRIM composition characterized by a lack of specific substrate binding domains, but contains in its helical domain a conserved sequence motif termed COS-box that has been speculated to fold independently into an α-hairpin. These characteristics had led to question whether MuRF1 adopts a canonical TRIM fold. Using a combination of electron paramagnetic resonance, on spin-labeled protein, and disulfide crosslinking, we show that TRIM63 follows the structural conservation of the TRIM dimerization domain, observed in other proteins. We also show that the COS-box motif folds back onto the dimerization coiled-coil motif, predictably forming a four-helical bundle at the center of the protein and emulating the architecture of canonical TRIMs.</dcterms:abstract>
    <dc:creator>Stevens, Michael</dc:creator>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2019-08-08T14:36:06Z</dc:date>
    <dcterms:title>Exploration of the TRIM Fold of MuRF1 Using EPR Reveals a Canonical Antiparallel Structure and Extended COS-Box</dcterms:title>
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    <dc:contributor>Mayans, Olga</dc:contributor>
    <dc:contributor>Cafiso, David  S.</dc:contributor>
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    <dc:creator>Skorupka, Katarzyna A.</dc:creator>
    <dc:creator>Mayans, Olga</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2019-08-08T14:36:06Z</dcterms:available>
    <dcterms:issued>2019-07-12</dcterms:issued>
    <dc:contributor>Skorupka, Katarzyna A.</dc:contributor>
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