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@ARTICLE{Kukuk:860088,
      author       = {Kukuk, Laura and Dingley, Andrew J. and Granzin, Joachim
                      and Nagel-Steger, Luitgard and Thiagarajan-Rosenkranz,
                      Pallavi and Ciupka, Daniel and Hänel, Karen and
                      Batra-Safferling, Renu and Pacheco, Victor and Stoldt,
                      Matthias and Pfeffer, Klaus and Beer-Hammer, Sandra and
                      Willbold, Dieter and Koenig, Bernd W.},
      title        = {{S}tructure of the {SL}y1 {SAM} homodimer reveals a new
                      interface for {SAM} domain self-association},
      journal      = {Scientific reports},
      volume       = {9},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2019-00874},
      pages        = {54},
      year         = {2019},
      abstract     = {Sterile alpha motif (SAM) domains are protein interaction
                      modules that are involved in a diverse range of biological
                      functions such as transcriptional and translational
                      regulation, cellular signalling, and regulation of
                      developmental processes. SH3 domain-containing protein
                      expressed in lymphocytes 1 (SLy1) is involved in immune
                      regulation and contains a SAM domain of unknown function. In
                      this report, the structure of the SLy1 SAM domain was solved
                      and revealed that this SAM domain forms a symmetric
                      homodimer through a novel interface. The interface consists
                      primarily of the two long C-terminal helices, α5 and
                      α5′, of the domains packing against each other. The
                      dimerization is characterized by a dissociation constant in
                      the lower micromolar range. A SLy1 SAM domain construct with
                      an extended N-terminus containing five additional amino
                      acids of the SLy1 sequence further increases the stability
                      of the homodimer, making the SLy1 SAM dimer two orders of
                      magnitude more stable than previously studied SAM
                      homodimers, suggesting that the SLy1 SAM dimerization is of
                      functional significance. The SLy1 SAM homodimer contains an
                      exposed mid-loop surface on each monomer, which may provide
                      a scaffold for mediating interactions with other SAM
                      domain-containing proteins via a typical
                      mid-loop–end-helix interface.},
      cin          = {ICS-6},
      ddc          = {600},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30631134},
      UT           = {WOS:000455352400037},
      doi          = {10.1038/s41598-018-37185-3},
      url          = {https://juser.fz-juelich.de/record/860088},
}