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High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds.

Abstract：

:Proteinaceous serine proteinase inhibitors are widespread throughout the plant kingdom where they play an important role in protection against pests and pathogens. Here, we describe the isolation and characterisation of a novel 14 amino acid residue cyclic peptide from sunflower seeds, which is a potent inhibitor of trypsin (Ki=100 pM). The crystal structure of this peptide in complex with bovine beta-trypsin shows both sequence and conformational similarity with the trypsin-reactive loop of the Bowman-Birk family of serine proteinase inhibitors. This inhibitor, however, is unique in being monofunctional, cyclic and far shorter (14 amino acid residues) than inhibitors belonging to this family (typically 60-70 amino acid residues). The high potency of this peptide is likely to arise from the considerable structural rigidity achieved through its cyclic nature which is further stabilised by a single internal disulphide bond. This study helps delineate the minimal unit required for effective peptide inhibitors of serine proteinases, and will assist in the further design of inhibitors to this widespread class of enzymes.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Luckett S,Garcia RS,Barker JJ,Konarev AV,Shewry PR,Clarke AR,Brady RL

doi

10.1006/jmbi.1999.2891

keywords:

subject

Has Abstract

pub_date

1999-07-09 00:00:00

pages

525-33

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92891-7

journal_volume

290

pub_type

杂志文章

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