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

研究成果: Contribution to journalArticle査読

89 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)413-420
ページ数8
ジャーナルFEBS Letters
269
2
DOI
出版ステータス出版済み - 9 3 1990
外部発表はい

All Science Journal Classification (ASJC) codes

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

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