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@ARTICLE{Deng:133926,
      author       = {Deng, X. and Morris, J. and Chaton, C. and Schröder,
                      Gunnar and Davidson, W. S. and Thompson, T. B.},
      title        = {{S}mall-angle {X}-ray {S}cattering of {A}polipoprotein
                      {A}-{IV} {R}eveals the {I}mportance of {I}ts {T}ermini for
                      {S}tructural {S}tability},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      number       = {7},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2013-02312},
      pages        = {4854 - 4866},
      year         = {2013},
      abstract     = {ApoA-IV is an amphipathic protein that can emulsify lipids
                      and has been linked to protective roles against
                      cardiovascular disease and obesity. We previously reported
                      an x-ray crystal structure of apoA-IV that was truncated at
                      its N and C termini. Here, we have extended this work by
                      demonstrating that self-associated states of apoA-IV are
                      stable and can be structurally studied using small-angle
                      x-ray scattering. Both the full-length monomeric and dimeric
                      forms of apoA-IV were examined, with the dimer showing an
                      elongated rod core with two nodes at opposing ends. The
                      monomer is roughly half the length of the dimer with a
                      single node. Small-angle x-ray scattering visualization of
                      several deletion mutants revealed that removal of both
                      termini can have substantial conformational effects
                      throughout the molecule. Additionally, the F334A point
                      mutation, which we previously showed increases apoA-IV lipid
                      binding, also exhibited large conformational effects on the
                      entire dimer. Merging this study's low-resolution structural
                      information with the crystal structure provides insight on
                      the conformation of apoA-IV as a monomer and as a dimer and
                      further defines that a clasp mechanism may control lipid
                      binding and, ultimately, protein function.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000315340400034},
      doi          = {10.1074/jbc.M112.436709},
      url          = {https://juser.fz-juelich.de/record/133926},
}