Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg

FEBS Letters

James, M.N.G.¹  McPhalen, C.A.¹  Schnebli, H.P.² 

[1] Medical Research Council of Canada in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada;Ciba-Geigy AG, CH-4002 Basel, Switzerland

关键词: Potato inhibitor 1;    Serine proteinase;    Molecular replacement method;    Hirudo medicinalis;    Crystallography;   

DOI  :  10.1016/0014-5793(85)80873-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of the molecular complex of eglin, a serine proteinase inhibitor from leeches, with subtilisin Carlsberg has been determined at 2.0 Å resolution by the molecular replacement method. The complex has been refined by restrained-parameter least-squares. The present crystallographic R factor (= Σ¦¦F _o¦-¦F _c¦/σ¦F _o¦) is 0.183. Eglin is a member of the potato inhibitor 1 family, a group of serine proteinase inhibitors lacking disulfide bonds. Eglin shows strong structural homology to CI-2, a related inhibitor from barley seeds. The structure of subtilisin Carlsberg in this complex is very similar to the known structure of subtilisin novo, despite changes of 84 out of 274 amino acids.

【 授权许可】

Unknown