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@ARTICLE{Pogenberg:139945,
      author       = {Pogenberg, V. and Oegmundsdottir, M. H. and
                      Bergsteinsdottir, K. and Schepsky, A. and Phung, B. and
                      Deineko, V. and Milewski, M. and Steingrimsson, E. and
                      Wilmanns, M. and DESY},
      title        = {{R}estricted leucine zipper dimerization and specificity of
                      {DNA} recognition of the melanocyte master regulator {MITF}},
      journal      = {Genes $\&$ development},
      volume       = {26},
      issn         = {0890-9369},
      address      = {Stanford, Calif.},
      publisher    = {HighWire Press},
      reportid     = {PHPPUBDB-24647},
      pages        = {2647-2658},
      year         = {2012},
      note         = {(c) Cold Spring Harbor Laboratory Press},
      abstract     = {Microphthalmia-associated transcription factor (MITF) is a
                      master regulator of melanocyte development and an important
                      oncogene in melanoma. MITF heterodimeric assembly with
                      related basic helix-loop-helix leucine zipper transcription
                      factors is highly restricted, and its binding profile to
                      cognate DNA sequences is distinct. Here, we determined the
                      crystal structure of MITF in its apo conformation and in the
                      presence of two related DNA response elements, the E-box and
                      M-box. In addition, we investigated mouse and human Mitf
                      mutations to dissect the functional significance of
                      structural features. Owing to an unusual three-residue shift
                      in the leucine zipper register, the MITF homodimer shows a
                      marked kink in one of the two zipper helices to allow an
                      out-of-register assembly. Removal of this insertion relieves
                      restricted heterodimerization by MITF and permits assembly
                      with the transcription factor MAX. Binding of MITF to the
                      M-box motif is mediated by an unusual nonpolar interaction
                      by Ile212, a residue that is mutated in mice and humans with
                      Waardenburg syndrome. As several related transcription
                      factors have low affinity for the M-box sequence, our
                      analysis unravels how these proteins discriminate between
                      similar target sequences. Our data provide a rational basis
                      for targeting MITF in the treatment of important hereditary
                      diseases and cancer.},
      keywords     = {Amino Acid Sequence / Animals / DNA-Binding Proteins:
                      chemistry / DNA-Binding Proteins: genetics / DNA-Binding
                      Proteins: metabolism / Dimerization / Enhancer Elements,
                      Genetic: genetics / Humans / Leucine Zippers: genetics /
                      Mice / Microphthalmia-Associated Transcription Factor:
                      chemistry / Microphthalmia-Associated Transcription Factor:
                      genetics / Microphthalmia-Associated Transcription Factor:
                      metabolism / Models, Molecular / Molecular Sequence Data /
                      Mutation / Protein Binding / Protein Structure, Tertiary /
                      Sequence Alignment / Waardenburg Syndrome: genetics /
                      DNA-Binding Proteins (NLM Chemicals) /
                      Microphthalmia-Associated Transcription Factor (NLM
                      Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW7 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW7-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23207919},
      pmc          = {pmc:PMC3521630},
      UT           = {WOS:000311944000008},
      doi          = {10.1101/gad.198192.112},
      url          = {https://bib-pubdb1.desy.de/record/139945},
}