% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Schillinger:836813,
      author       = {Schillinger, Oliver and Panwalkar, Vineet and Strodel,
                      Birgit and Dingley, Andrew},
      title        = {{M}olecular {D}ynamics {S}imulations {R}eveal {K}ey {R}oles
                      of the {I}nterleukin-6 {A}lpha {R}eceptor in the {A}ssembly
                      of the {H}uman {I}nterleukin-6 {R}eceptor {C}omplex},
      journal      = {The journal of physical chemistry letters},
      volume       = {121},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2017-05855},
      pages        = {8113-8122},
      year         = {2017},
      abstract     = {Human interleukin-6 (hIL-6) is a pleiotropic cytokine with
                      three distinct receptor epitopes, termed sites I, II and
                      III, which function to assemble a signaling complex. hIL-6
                      signals via a glycoprotein 130 (gp130) homodimer after
                      initially forming a heterodimer with the non-signaling
                      α-receptor (IL-6Rα). The molecular description of the
                      assembly of the hIL-6 signaling complex remains elusive
                      because available structures provide descriptions of hIL-6
                      in its free and fully bound receptor forms, but not for
                      intermediate steps that are crucial in the stepwise assembly
                      of the signaling complex. In this report, molecular dynamics
                      simulations provide atomic details describing the functional
                      role of the initial hIL-6/IL-6Rα complex in facilitating
                      subsequent interactions with gp130, which have not been
                      previously shown. IL-6Rα binding to hIL-6 rigidifies the
                      flexible N-terminus of the hIL-6 AB-loop through
                      interactions with the D2 domain of IL-6Rα. This
                      rigidification combined with repositioning of residues
                      involved in gp130 receptor recognition promotes gp130
                      binding at site III. Binding of gp130 receptors at sites II
                      and III is coupled with the release of the hIL-6 N-terminal
                      AB-loop interaction and a pivoting of IL-6Rα around the
                      hIL-6 helix bundle to the state of the hIL-6/IL-6Rα/gp130
                      complex.},
      cin          = {ICS-6},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000409394900011},
      doi          = {10.1021/acs.jpcb.7b05732},
      url          = {https://juser.fz-juelich.de/record/836813},
}