Gáspári Zoltán, Ortutay Csaba, Perczel András
Department of Organic Chemistry, Eötvös University, Pázmány Péter sétány 1/A, Budapest, Hungary.
Bioinformatics. 2004 Mar 1;20(4):448-51. doi: 10.1093/bioinformatics/btg451. Epub 2004 Jan 22.
Members of the pacifastin family are small, approximately 35-residue serine protease inhibitors isolated from arthropod species. Several locust inhibitors exhibit intriguing taxon specificity while others do not. The structural basis of this phenomenon may lie in the different dynamical properties of the proteins originating from different stabilizing interactions. In this study, we identify new members of the family to confirm the universal role of these interactions in the family. Structural investigations show that both the disulfide pattern and the stabilizing interactions are unique among small all-beta proteins.
pacifastin家族的成员是从小节肢动物物种中分离出来的小型蛋白质，约含35个氨基酸残基，是丝氨酸蛋白酶抑制剂。几种蝗虫抑制剂表现出有趣的分类群特异性，而其他的则没有。这种现象的结构基础可能在于源自不同稳定相互作用的蛋白质具有不同的动力学特性。在本研究中，我们鉴定出该家族的新成员，以证实这些相互作用在该家族中的普遍作用。结构研究表明，二硫键模式和稳定相互作用在所有小型全β蛋白中都是独特的。
