The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold [v1; ref status: indexed, http://f1000r.es/1dq]

The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold [v1; ref status: indexed, http://f1000r.es/1dq]

We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold....

Full description

Bibliographic Details
Main Authors: Daniel J Rigden, Qingping Xu, Yuanyuan Chang, Ruth Y Eberhardt, Robert D Finn, Neil D Rawlings
Format: Article
Language:English
Published: F1000 Research Ltd 2013-07-01
Series:F1000Research
Subjects:
Protein Folding
Structural Genomics
Online Access:http://f1000research.com/articles/2-154/v1

Internet

http://f1000research.com/articles/2-154/v1

Similar Items