CRYSTALLIZATION AND INITIAL CRYSTALLOGRAPHIC RESULTS FOR PEPSTATIN-A INHIBITED BOVINE CATHEPSIN-D

被引：4

作者：

BIEBER, F ^{[1
]}

BRACHVOGEL, V ^{[1
]}

ARNI, R ^{[1
]}

FUSEK, M ^{[1
]}

METCALF, P ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1,POSTFACH 10-2209,W-6900 HEIDELBERG,GERMANY

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 227卷 / 04期

关键词：

CATHEPSIN-D; PEPSTATIN; ASPARTIC PROTEASE; LYSOSOMAL TARGETING; CRYSTAL;

D O I：

10.1016/0022-2836(92)90539-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cathepsin D was purified from bovine liver by a method using two pepstatin A affinity columns. The eluted protein was combined with pepstatin A and the complex crystallized from 15% polyethylene glycol 8000 at pH 5·9. The crystals diffract to a resolution of 3·0 Å and have space group P212121 with unit cell dimensions a = 74·8 A ̊, b = 76·0 A ̊, c = 157·7 A ̊. There are two molecules in the asymmetric unit. The structure was solved by molecular replacement using a pepsin search model and both molecules showed clearly interpretable density in the position expected for pepstatin A in a preliminary difference map. The refined model has r.m.s. deviations from ideal bond lengths and angles of 0·014 Å and 3·2 °, respectively, and a crystallographic `R factor of 17%. © 1992.

引用

页码：1265 / 1268

页数：4

共 19 条

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