Wei A Z, Mayr I, Bode W
Max-Planck-Institut für Biochemie, Martinsried, FRG.
FEBS Lett. 1988 Jul 18;234(2):367-73. doi: 10.1016/0014-5793(88)80118-2.
The stoichiometric complex formed between human leukocyte elastase and a synthetic MeO-Suc-Ala-Ala-Pro-Val chloromethyl ketone inhibitor was co-crystallized and its X-ray structure determined, using Patterson search methods. Its structure has been crystallographically refined to a final R value of 0.145 (8.0 and 2.3 A). The enzyme structure is very similar to that recently observed in a complex formed with the ovomucoid third domain from turkey [(1986) EMBO J. 5,2453-2458]. The rms deviation of all alpha-carbon atoms is 0.32 A. The peptidic inhibitor is bound in a similar overall conformation as the ovomucoid binding segment. Covalent bonds are formed between Val-P1 of the inhibitor and His-57 NE2 and Ser-195 OG of the enzyme. The carbonyl carbon is tetrahedrally deformed to a hemiketal. The valine side chain is arranged in the S1 pocket in the g-conformation.
使用帕特森搜索方法，使人白细胞弹性蛋白酶与合成的甲氧基琥珀酰 - 丙氨酰 - 丙氨酰 - 脯氨酰 - 缬氨酰氯甲基酮抑制剂形成的化学计量复合物共结晶，并确定其X射线结构。其结构已通过晶体学方法精修至最终R值为0.145（8.0和2.3埃）。该酶的结构与最近在与来自火鸡的卵类粘蛋白第三结构域形成的复合物中观察到的结构非常相似[（1986年）《欧洲分子生物学组织杂志》5，2453 - 2458]。所有α - 碳原子的均方根偏差为0.32埃。肽类抑制剂以与卵类粘蛋白结合片段相似的总体构象结合。抑制剂的缬氨酸 - P1与酶的组氨酸 - 57 NE2和丝氨酸 - 195 OG之间形成共价键。羰基碳四面体变形为半缩酮。缬氨酸侧链以g - 构象排列在S1口袋中。
