Baumann U, Bode W, Huber R, Travis J, Potempa J
Max-Planck-Institut für Biochemie, Martinsried bei München, Germany.
J Mol Biol. 1992 Aug 20;226(4):1207-18. doi: 10.1016/0022-2836(92)91062-t.
The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.
丝氨酸蛋白酶抑制剂超家族成员——活性位点裂解的马白细胞弹性蛋白酶抑制剂的晶体结构已得到解析，并在1.95埃分辨率下精修至晶体学R因子为17.6%。尽管它是一种细胞内抑制剂，与人类α1 -抗糜蛋白酶和α1 -蛋白酶抑制剂的序列同源性相当低，仅为30%，但其三维结构非常相似，仅在插入位点和少数可变二级结构元件处存在偏差。与其他裂解丝氨酸蛋白酶抑制剂的结构相比，更高的分辨率使得对丝氨酸蛋白酶抑制剂所谓的R态能够进行更精确的描述。
