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@ARTICLE{Erat:151882,
      author       = {Erat, M. C. and Sladek, B. and Campbell, I. D. and
                      Vakonakis, I. and DESY},
      title        = {{S}tructural {A}nalysis of {C}ollagen {T}ype {I}
                      {I}nteractions with {H}uman {F}ibronectin {R}eveals a
                      {C}ooperative {B}inding {M}ode},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      number       = {24},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PHPPUBDB-26532},
      pages        = {17441 - 17450},
      year         = {2013},
      note         = {© by The American Society for Biochemistry and Molecular
                      Biology, Inc.},
      abstract     = {Despite its biological importance, the interaction between
                      fibronectin (FN) and collagen, two abundant and crucial
                      tissue components, has not been well characterized on a
                      structural level. Here, we analyzed the four interactions
                      formed between epitopes of collagen type I and the
                      collagen-binding fragment (gelatin-binding domain (GBD)) of
                      human FN using solution NMR, fluorescence, and small angle
                      x-ray scattering methods. Collagen association with FN
                      modules (8-9)FnI occurs through a conserved structural
                      mechanism but exhibits a 400-fold disparity in affinity
                      between collagen sites. This disparity is reduced in the
                      full-length GBD, as (6)FnI(1-2)FnII(7)FnI binds a specific
                      collagen epitope next to the weakest (8-9)FnI-binding site.
                      The cooperative engagement of all GBD modules with collagen
                      results in four broadly equipotent FN-collagen interaction
                      sites. Collagen association stabilizes a distinct monomeric
                      GBD conformation in solution, giving further evidence to the
                      view that FN fragments form well defined functional and
                      structural units.},
      cin          = {DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {DORIS Beamline D1.2 (POF1-550)},
      pid          = {G:(DE-H253)POF1-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000320380600036},
      pubmed       = {pmid:23653354},
      doi          = {10.1074/jbc.M113.469841},
      url          = {https://bib-pubdb1.desy.de/record/151882},
}