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 |
巻 | 269 |
号 | 2 |
DOI | |
出版ステータス | 出版済み - 9月 3 1990 |
外部発表 | はい |
All Science Journal Classification (ASJC) codes
- 生物理学
- 構造生物学
- 生化学
- 分子生物学
- 遺伝学
- 細胞生物学