Structure basis for the unique specificity of medaka enteropeptidase light chain

Hao Wang,Jin Xu,Xiaoze Wang,Shi Hu,Yajun Guo,Xinyue Zhang,Ziye Zhao,Dapeng Zhang

doi:10.1007/s13238-013-0008-x

Abstract

Structure basis for the unique specificity of medaka enteropeptidase light chain

Highlights

Dear Editor, Enteropeptidase is a serine protease, which shows a specific cleavage of its substrates at the C-terminal of the recognition site (Asp)4Lys (Zheng et al, 2009)
Shahravan et al showed that bovine enteropeptidase light chain (BEPL) cleaved at unexpected DR and SR sites in AhR6-C/EBP protein (Shahravan et al, 2008)
The crystal structure of MEPL was determined by molecular replacement using the bovine enteropeptidase light chain (PDB entry 1EKB, 53.7% amino acid identity) as the search model and refined to 2.0 Å resolution

Summary

Introduction

Dear Editor, Enteropeptidase (enterokinase, EC 3.4.21.9) is a serine protease, which shows a specific cleavage of its substrates at the C-terminal of the recognition site (Asp)4Lys (Zheng et al, 2009). The recombinant bovine enteropeptidase light chain (BEPL) is most commonly used. We sought to solve the crystal structure of the light chain of medaka enteropeptidase (MEPL), and gain insights into the determinants for its stricter specificity.

Results

Conclusion