STRUCTURE OF A PEPSIN RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR
STRUCTURE OF A PEPSIN RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR
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DOI：
10.1107/s0108768192001939
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发表时间：
1992-08-01
影响因子：
1.9
通讯作者：
ABADZAPATERO, C
中科院分区：
文献类型：
--
作者：
CHEN, LQ;ERICKSON, JW;ABADZAPATERO, C
用分子置换法测定了一种单斜晶系的胃蛋白酶/肾素抑制剂复合物晶体的结构，该晶体的不对称单元中含有两个分子。原子模型，由两个配体胃蛋白酶分子和110个水分子，已被细化到最终的晶体学R值为0。139用于8和2.9埃分辨率之间的数据。该结构揭示了以前未描述的胃蛋白酶二聚体主要通过极性相互作用形成。抑制剂结合诱导全局结构变化的天然酶类似，但不相同，在其他化学上类似的胃蛋白酶/肾素抑制剂复合物中观察到的正交晶型结晶。在正交晶体中不可见的多肽链区域（残基292-297）在目前描述的结构中是有序的;可能由晶体接触诱导。天然胃蛋白酶的晶体包装进行了比较，两种不同的晶体形式的抑制酶。
The structure determination by molecular replacement methods of a monoclinic pepsin/renin inhibitor complex crystal, with two molecules in the asymmetric unit, is presented. The atomic model, consisting of two liganded pepsin molecules and 110 water molecules, has been refined to a final crystallographic R value of 0. 139 for data between 8 and 2.9 angstrom resolution. The structure reveals a previously undescribed pepsin dimer formed predominantly by polar interactions. Inhibitor binding induces global structural changes in the native enzyme similar, but not identical, to the ones observed in other chemically similar pepsin/renin inhibitor complexes crystallized in an orthorhombic form. A region of the polypeptide chain (residues 292-297) which was not visible in the orthorhombic crystal is well ordered in the presently described structure; possibly induced by crystal contacts. The crystal packing of native pepsin is compared with the two different crystal forms of the inhibited enzyme.