Simonovic M, Gettins P G, Volz K
Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612-7334, USA.
Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1440-2. doi: 10.1107/s0907444900009884.
CrmA is an unusual serpin that has a reactive-center loop one residue shorter than other members of the superfamily. Most interestingly, crmA has inhibitory activity against both cysteine and serine proteinases involved in the regulation of cell apoptosis. The three-dimensional structure of crmA will give insight into the mechanism that this serpin employs to inhibit both cysteine and the serine proteinases, as well as help to explain the significance of the shorter reactive-center loop. The monodisperse cysteine-free mutant of crmA was crystallized in the presence of phosphate salts. Crystals diffract to 2.90 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.67, b = 93.15, c = 101.63 A.
CrmA是一种不同寻常的丝氨酸蛋白酶抑制剂，其反应中心环比该超家族的其他成员短一个残基。最有趣的是，CrmA对参与细胞凋亡调节的半胱氨酸蛋白酶和丝氨酸蛋白酶都具有抑制活性。CrmA的三维结构将有助于深入了解这种丝氨酸蛋白酶抑制剂抑制半胱氨酸蛋白酶和丝氨酸蛋白酶的机制，并有助于解释较短的反应中心环的意义。无半胱氨酸的单分散CrmA突变体在磷酸盐存在下结晶。晶体衍射至2.90埃，属于空间群P2(1)2(1)2(1)，晶胞参数a = 42.67，b = 93.15，c = 101.63埃。
