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@ARTICLE{Boix:144054,
      author       = {Boix, E. and Pulido, D. and Moussaoui, M. and Nogues, M. V.
                      and Russi, S. and DESY},
      title        = {{T}he sulfate-binding site structure of the human
                      eosinophil cationic protein as revealed by a new crystal
                      form},
      journal      = {Journal of structural biology},
      volume       = {179},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-25783},
      pages        = {1-9},
      year         = {2012},
      abstract     = {The human eosinophil cationic protein (ECP), also known as
                      RNase 3, is an eosinophil secretion protein that is involved
                      in innate immunity and displays antipathogen and
                      proinflammatory activities. ECP has a high binding affinity
                      for heterosaccharides, such as bacterial lipopolysaccharides
                      and heparan sulfate found in the glycocalix of eukaryotic
                      cells. We have crystallized ECP in complex with sulfate
                      anions in a new monoclinic crystal form. In this form, the
                      active site groove is exposed, providing an alternative
                      model for ligand binding studies. By exploring the
                      protein-sulfate complex, we have defined the sulfate binding
                      site architecture. Three main sites (S1-S3) are located in
                      the protein active site; S1 and S2 overlap with the
                      phosphate binding sites involved in RNase nucleotide
                      recognition. A new site (S3) that is unique to ECP is one of
                      the key anchoring points for sulfated ligands. Arg 1 and Arg
                      7 in S3, together with Arg 34 and Arg 36 in S1, form the
                      main basic clusters that assist in the recognition of ligand
                      anionic groups. The location of additional sulfate bound
                      molecules, some of which contribute to the crystal packing,
                      may mimic the binding to extended anionic polymers. In
                      conclusion, the structural data define a binding pattern for
                      the recognition of sulfated molecules that can modulate the
                      role of ECP in innate immunity. The results reveal the
                      structural basis for the high affinity of ECP for
                      glycosaminoglycans and can assist in structure-based drug
                      design of inhibitors of the protein cytotoxicity to host
                      tissues during inflammation.},
      keywords     = {Amino Acid Sequence / Catalytic Domain / Crystallization /
                      Eosinophil Cationic Protein: chemistry / Eosinophil Cationic
                      Protein: metabolism / Glycosaminoglycans: chemistry /
                      Glycosaminoglycans: metabolism / Humans / Ligands /
                      Molecular Dynamics Simulation / Molecular Sequence Data /
                      Protein Binding / Protein Conformation / Recombinant
                      Proteins: chemistry / Recombinant Proteins: metabolism /
                      Sulfates: chemistry / Glycosaminoglycans (NLM Chemicals) /
                      Ligands (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Sulfates (NLM Chemicals) / Eosinophil Cationic
                      Protein (NLM Chemicals)},
      cin          = {HASYLAB},
      ddc          = {540},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
      pnm          = {DORIS Beamline K1.1 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.1-20130405},
      experiment   = {EXP:(DE-H253)D-K1.1-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22579681},
      UT           = {WOS:000305775400001},
      doi          = {10.1016/j.jsb.2012.04.023},
      url          = {https://bib-pubdb1.desy.de/record/144054},
}