1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

Hiroyuki Hanzawa, Ichio Shimada, Takashi Kuzuhara, Hiroto Komano, Daisuke Kohda, Fuyuhiko Inagaki, Shunji Natori, Yoji Arata

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Abstract

The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.

Original languageEnglish
Pages (from-to)413-420
Number of pages8
JournalFEBS Letters
Volume269
Issue number2
DOIs
Publication statusPublished - Sep 3 1990
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Hanzawa, H., Shimada, I., Kuzuhara, T., Komano, H., Kohda, D., Inagaki, F., Natori, S., & Arata, Y. (1990). 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin. FEBS Letters, 269(2), 413-420. https://doi.org/10.1016/0014-5793(90)81206-4