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@ARTICLE{Mortensen:328781,
      author       = {Mortensen, Sofia and Kidmose, Rune T. and Petersen, Steen
                      V. and Szilágyi, Ágnes and Prohászka, Zoltan and
                      Andersen, Gregers R.},
      title        = {{S}tructural {B}asis for the {F}unction of {C}omplement
                      {C}omponent {C}4 within the {C}lassical and {L}ectin
                      {P}athways of {C}omplement},
      journal      = {The journal of immunology},
      volume       = {194},
      number       = {11},
      issn         = {1550-6606},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PUBDB-2017-05441},
      pages        = {5488 - 5496},
      year         = {2015},
      abstract     = {Complement component C4 is a central protein in the
                      classical and lectin pathways within the complement system.
                      During activation of complement, its major fragment C4b
                      becomes covalently attached to the surface of pathogens and
                      altered self-tissue, where it acts as an opsonin marking the
                      surface for removal. Moreover, C4b provides a platform for
                      assembly of the proteolytically active convertases that
                      mediate downstream complement activation by cleavage of C3
                      and C5. In this article, we present the crystal and solution
                      structures of the 195-kDa C4b. Our results provide the
                      molecular details of the rearrangement accompanying C4
                      cleavage and suggest intramolecular flexibility of C4b. The
                      conformations of C4b and its paralogue C3b are shown to be
                      remarkably conserved, suggesting that the convertases from
                      the classical and alternative pathways are likely to share
                      their overall architecture and mode of substrate
                      recognition. We propose an overall molecular model for the
                      classical pathway C5 convertase in complex with C5,
                      suggesting that C3b increases the affinity for the substrate
                      by inducing conformational changes in C4b rather than a
                      direct interaction with C5. C4b-specific features revealed
                      by our structural studies are probably involved in the
                      assembly of the classical pathway C3/C5 convertases and C4b
                      binding to regulators.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000354905300049},
      pubmed       = {pmid:25911760},
      doi          = {10.4049/jimmunol.1500087},
      url          = {https://bib-pubdb1.desy.de/record/328781},
}