Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1990 Sep 3;269(2):413-20. doi: 10.1016/0014-5793(90)81206-4.
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.
通过1H核磁共振（NMR）和动态模拟退火计算确定了一种抗菌蛋白沙佩辛（sapecin）的溶液构象。结果表明，该多肽折叠结构由一个柔性环（第4 - 12位残基）、一个螺旋（第15 - 23位残基）和两条延伸链（第24 - 31位残基和第34 - 40位残基）组成。研究发现，沙佩辛的三级结构与兔中性粒细胞防御素NP - 5完全不同，后者在氨基酸序列上与沙佩辛同源且也具有抗菌活性。三维结构测定显示，在沙佩辛表面，一个富含碱性残基的区域和疏水表面相互面对。
