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@ARTICLE{Berbs:119641,
      author       = {M. Á. Berbís and S. André and F. J. Cañada and R.
                      Pipkorn$^*$ and H. Ippel and K. H. Mayo and D. Kübler$^*$
                      and H.-J. Gabius and J. Jiménez-Barbero},
      title        = {{P}eptides derived from human galectin-3 {N}-terminal tail
                      interact with its carbohydrate recognition domain in a
                      phosphorylation-dependent manner.},
      journal      = {Biochemical and biophysical research communications},
      volume       = {443},
      number       = {1},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {DKFZ-2017-00272},
      pages        = {126 - 131},
      year         = {2014},
      abstract     = {Galectin-3 (Gal-3) is a multi-functional effector protein
                      that functions in the cytoplasm and the nucleus, as well as
                      extracellularly following non-classical secretion.
                      Structurally, Gal-3 is unique among galectins with its
                      carbohydrate recognition domain (CRD) attached to a rather
                      long N-terminal tail composed mostly of collagen-like
                      repeats (nine in the human protein) and terminating in a
                      short non-collagenous terminal peptide sequence unique in
                      this lectin family and not yet fully explored. Although
                      several Ser and Tyr sites within the N-terminal tail can be
                      phosphorylated, the physiological significance of this
                      post-translational modification remains unclear. Here, we
                      used a series of synthetic (phospho)peptides derived from
                      the tail to assess phosphorylation-mediated interactions
                      with (15)N-labeled Gal-3 CRD. HSQC-derived chemical shift
                      perturbations revealed selective interactions at the
                      backface of the CRD that were attenuated by phosphorylation
                      of Tyr 107 and Tyr 118, while phosphorylation of Ser 6 and
                      Ser 12 was essential. Controls with sequence scrambling
                      underscored inherent specificity. Our studies shed light on
                      how phosphorylation of the N-terminal tail may impact on
                      Gal-3 function and prompt further studies using
                      phosphorylated full-length protein.},
      keywords     = {Carbohydrates (NLM Chemicals) / Galectin 3 (NLM Chemicals)
                      / Peptides (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Tyrosine (NLM Chemicals)},
      cin          = {D015 / A060},
      ddc          = {570},
      cid          = {I:(DE-He78)D015-20160331 / I:(DE-He78)A060-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24269589},
      doi          = {10.1016/j.bbrc.2013.11.063},
      url          = {https://inrepo02.dkfz.de/record/119641},
}