Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata.

@article{Hemmi2005StructuralAF,
  title={Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata.},
  author={H. Hemmi and T. Kumazaki and K. Yoshizawa-Kumagaye and Y. Nishiuchi and Takuya Yoshida and T. Ohkubo and Yuji Kobayashi},
  journal={Biochemistry},
  year={2005},
  volume={44 28},
  pages={
          9626-36
        }
}
Anemonia elastase inhibitor (AEI) is a "nonclassical" Kazal-type elastase inhibitor from Anemonia sulcata. Unlike many nonclassical inhibitors, AEI does not have a cystine-stabilized alpha-helical (CSH) motif in the sequence. We chemically synthesized AEI and determined its three-dimensional solution structure by two-dimensional NMR spectroscopy. The resulting structure of AEI was characterized by a central alpha-helix and a three-stranded antiparallel beta-sheet of a typical Kazal-type… Expand
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  • Chemistry, Medicine
  • Comparative biochemistry and physiology. Part A, Molecular & integrative physiology
  • 2007
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