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@ARTICLE{Banci:96611,
      author       = {Banci, L. and Bertini, I. and Boca, M. and Calderone, V.
                      and Cantini, F. and Girotto, S. and Vieru, M. and DESY},
      title        = {{S}tructural and dynamic aspects related to oligomerization
                      of apo {SOD}1 and its mutants.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {106},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PHPPUBDB-20353},
      pages        = {6980-6985},
      year         = {2009},
      abstract     = {The structural and dynamical properties of the metal-free
                      form of WT human superoxide dismutase 1 (SOD1) and its
                      familial amyotrophic lateral sclerosis (fALS)-related
                      mutants, T54R and I113T, were characterized both in
                      solution, through NMR, and in the crystal, through X-ray
                      diffraction. We found that all 3 X-ray structures show
                      significant structural disorder in 2 loop regions that are,
                      at variance, well defined in the fully-metalated structures.
                      Interestingly, the apo state crystallizes only at low
                      temperatures, whereas all 3 proteins in the metalated form
                      crystallize at any temperature, suggesting that
                      crystallization selects one of the most stable conformations
                      among the manifold adopted by the apo form in solution.
                      Indeed, NMR experiments show that the protein in solution is
                      highly disordered, sampling a large range of conformations.
                      The large conformational variability of the apo state allows
                      the free reduced cysteine Cys-6 to become highly solvent
                      accessible in solution, whereas it is essentially buried in
                      the metalated state and the crystal structures. Such solvent
                      accessibility, together with that of Cys-111, accounts for
                      the tendency to oligomerization of the metal-free state. The
                      present results suggest that the investigation of the
                      solution state coupled with that of the crystal state can
                      provide major insights into SOD1 pathway toward
                      oligomerization in relation to fALS.},
      keywords     = {Apoproteins: chemistry / Apoproteins: genetics /
                      Apoproteins: metabolism / Crystallography, X-Ray / Humans /
                      Models, Molecular / Mutation: genetics / Nuclear Magnetic
                      Resonance, Biomolecular / Protein Multimerization / Protein
                      Structure, Quaternary / Protein Structure, Secondary /
                      Protein Structure, Tertiary / Superoxide Dismutase:
                      chemistry / Superoxide Dismutase: genetics / Superoxide
                      Dismutase: metabolism / Apoproteins (NLM Chemicals) /
                      superoxide dismutase 1 (NLM Chemicals) / Superoxide
                      Dismutase (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {000},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW7 (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW7-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19369197},
      pmc          = {pmc:PMC2678485},
      UT           = {WOS:000265584500022},
      doi          = {10.1073/pnas.0809845106},
      url          = {https://bib-pubdb1.desy.de/record/96611},
}