Shimamoto T, Shimamoto T, Okada Y, Yamada N, Miyata K, Kiho Y
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Cell Struct Funct. 1991 Feb;16(1):31-8. doi: 10.1247/csf.16.31.
The interaction between surface proteins of some enveloped viruses and trypsin was studied by computer analysis. Prior to the cleavage of the viral protein by trypsin, hydrophobic interaction between them at the vicinity of their active sites may occur. An exposed hydrophobic portion was found there which theoretically could stimulate the interaction. This interaction would be rather non-specific: according to the analysis, trypsin could bind equally well with weakly virulent virus and virulent viruses. Following this interaction, a specific reaction between their active sites would occur. The specificity was found to be related to the virulency of the virus.
通过计算机分析研究了一些包膜病毒表面蛋白与胰蛋白酶之间的相互作用。在胰蛋白酶切割病毒蛋白之前，它们在活性位点附近可能会发生疏水相互作用。在那里发现了一个暴露的疏水部分，理论上它可以刺激这种相互作用。这种相互作用相当非特异性：根据分析，胰蛋白酶与弱毒病毒和强毒病毒结合的效果相当。这种相互作用之后，它们的活性位点之间会发生特异性反应。发现这种特异性与病毒的毒力有关。
