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@ARTICLE{Gudez:580693,
      author       = {Guédez, Gabriela and Loers, Gabriele and Jeffries, Cy M.
                      and Kozak, Sandra and Meijers, Rob and Svergun, Dmitri I.
                      and Schachner, Melitta and Loew, Christian},
      title        = {{X}‐ray structure and function of fibronectin domains two
                      and three of the neural cell adhesion molecule {L}1},
      journal      = {The FASEB journal},
      volume       = {37},
      number       = {3},
      issn         = {0892-6638},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PUBDB-2023-01383},
      pages        = {e22823},
      year         = {2023},
      abstract     = {The cell adhesion molecule L1 (L1CAM, L1 in short) plays
                      crucial roles during neural development, regeneration after
                      injury, synapse formation, synaptic plasticity and tumor
                      cell migration. L1 belongs to the immunoglobulin superfamily
                      and comprises in its extracellular part six immunoglobulin
                      (Ig)-like domains and five fibronectin type III homologous
                      repeats (FNs). The second Ig-like domain has been validated
                      for self- (so-called homophilic) binding between cells.
                      Antibodies against this domain inhibit neuronal migration in
                      vitro and in vivo. The fibronectin type III homologous
                      repeats FN2 and FN3 bind small molecule agonistic L1
                      mimetics and contribute to signal transduction. FN3 has a
                      stretch of 25 amino acids that can be triggered with a
                      monoclonal antibody, or the L1 mimetics, to enhance neurite
                      outgrowth and neuronal cell migration in vitro and in vivo.
                      To correlate the structural features of these FNs with
                      function, we determined a high-resolution crystal structure
                      of a FN2FN3 fragment, which is functionally active in
                      cerebellar granule cells and binds several mimetics. The
                      structure illustrates that both domains are connected by a
                      short linker sequence allowing a flexible and largely
                      independent organization of both domains. This becomes
                      further evident by comparing the X-ray crystal structure
                      with models derived from Small-Angle X-ray Scattering (SAXS)
                      data for FN2FN3 in solution. Based on the X-ray crystal
                      structure, we identified five glycosylation sites which we
                      believe are crucial for folding and stability of these
                      domains. Our study signifies an advance in the understanding
                      of structure–functional relationships of L1.},
      cin          = {EMBL-User / EMBL / CSSB-EMBL / CSSB-EMBL-CL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731 /
                      I:(DE-H253)CSSB-EMBL-20141216 /
                      I:(DE-H253)CSSB-EMBL-CL-20210806},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101 / EXP:(DE-H253)P-P13-20150101 /
                      EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36809668},
      UT           = {WOS:000936837500001},
      doi          = {10.1096/fj.202201511R},
      url          = {https://bib-pubdb1.desy.de/record/580693},
}