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@ARTICLE{Recktenwald:607076,
      author       = {Recktenwald, Christian V. and Karlsson, Göran and
                      Garcia-Bonete, Maria-Jose and Katona, Gergely and Jensen,
                      Maja and Lymer, Richard and Bäckström, Malin and
                      Johansson, Malin E. V. and Hansson, Gunnar C. and
                      Trillo-Muyo, Sergio},
      title        = {{T}he structure of the second {C}ys{D} domain of {MUC}2 and
                      role in mucin organization by transglutaminase-based
                      cross-linking},
      journal      = {Cell reports},
      volume       = {43},
      number       = {5},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-01774},
      pages        = {114207},
      year         = {2024},
      abstract     = {The MUC2 mucin protects the colonic epithelium by a
                      two-layered mucus with an inner attached bacteria-free layer
                      and an outer layer harboring commensal bacteria. CysD
                      domains are 100 amino-acid-long sequences containing 10
                      cysteines that separate highly O-glycosylated proline,
                      threonine, serine (PTS) regions in mucins. The structure of
                      the second CysD, CysD2, of MUC2 is now solved by nuclear
                      magnetic resonance. CysD2 shows a stable stalk region
                      predicted to be partly covered by adjacent O-glycans
                      attached to neighboring PTS sequences, whereas the CysD2 tip
                      with three flexible loops is suggested to be well exposed.
                      It shows transient dimer interactions at acidic pH, weakened
                      at physiological pH. This transient interaction can be
                      stabilized in vitro and in vivo by transglutaminase
                      3-catalyzed isopeptide bonds, preferring a specific
                      glutamine residue on one flexible loop. This covalent dimer
                      is modeled suggesting that CysD domains act as connecting
                      hubs for covalent stabilization of mucins to form a
                      protective mucus.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38733585},
      UT           = {WOS:001240463800001},
      doi          = {10.1016/j.celrep.2024.114207},
      url          = {https://bib-pubdb1.desy.de/record/607076},
}