1L4V

SOLUTION STRUCTURE OF SAPECIN

1L4V の概要

• エントリーDOI: 10.2210/pdb1l4v/pdb
• 分子名称: Sapecin (1 entity in total)
• 機能のキーワード: antibacterial protein, insect defensin, antibiotic
• 由来する生物種: Sarcophaga peregrina
• 細胞内の位置: Secreted: P18313
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4086.71

構造登録者

Hanzawa, H.,Iwai, H.,Takeuchi, K.,Kuzuhara, T.,Komano, H.,Kohda, D.,Inagaki, F.,Natori, S.,Arata, Y.,Shimada, I. (登録日: 2002-03-06, 公開日: 2002-03-27, 最終更新日: 2024-10-30)

主引用文献

Hanzawa, H.,Shimada, I.,Kuzuhara, T.,Komano, H.,Kohda, D.,Inagaki, F.,Natori, S.,Arata, Y.
1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.
FEBS Lett., 269:413-420, 1990

PubMed 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.

PubMed: 2401368
DOI: 10.1016/0014-5793(90)81206-4

実験手法

SOLUTION NMR