Purification and crystallization of the extracellular domain of human neutral endopeptidase (neprilysin) expressed in Pichia pastoris

被引：10

作者：

Dale, GE ^{[1
]}

D'Arcy, B ^{[1
]}

Yuvaniyama, C ^{[1
]}

Wipf, B ^{[1
]}

Oefner, C ^{[1
]}

D'Arcy, A ^{[1
]}

机构：

[1] F Hoffmann La Roche & Co Ltd, Preclin Res, CH-4070 Basel, Switzerland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900004947

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Neutral endopeptidase (NEP) is a mammalian zinc metalloprotease involved in the inactivation of a wide variety of regulatory peptides such as enkephalins and atrial natiuretic factor. The soluble extracellular domain of NEP (sNEP) was expressed in the methylotrophic yeast Pichia pastoris. The protein was purified to homogeneity and single crystals have been obtained. Enzymatic deglycosylation of the enzyme was essential for the production of crystals suitable for X-ray analysis for both the NEP-phosphoramidon binary complex and the apo enzyme.

引用

页码：894 / 897

页数：4

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