Crystallographic structure of a complex between trypsin and a nonapeptide derived from a Bowman-Birk inhibitor found in Vigna unguiculata seeds.
Bowman-Birk inhibitors
Breast cancer
Protease inhibitors
Protein crystallographic structure
Vigna unguiculata
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 04 2019
15 04 2019
Historique:
received:
27
12
2018
revised:
16
02
2019
accepted:
18
02
2019
pubmed:
1
3
2019
medline:
15
2
2020
entrez:
1
3
2019
Statut:
ppublish
Résumé
Natural inhibitors of proteases have been classified into different families, among them is the Bowman-Birk Inhibitor (BBI) family. Members of BBI have two structurally reactive loops that simultaneously inhibit trypsin and chymotrypsin. Here, we have investigated the binding of bovine trypsin by a cyclic nonapeptide, named PTRY9 (CTKSIPPQC), derived of the black-eyed pea trypsin/chymotrypsin inhibitor (BTCI) from Vigna unguiculata seeds. This peptide was synthetically produced with the disulfide bond restraining its conformation to mimic the reactive loop that inhibits trypsin. PTRY9 complexed to pancreatic bovine trypsin was crystallized in orthorhombic and trigonal space groups, P2
Identifiants
pubmed: 30817908
pii: S0003-9861(18)31052-X
doi: 10.1016/j.abb.2019.02.013
pii:
doi:
Substances chimiques
Oligopeptides
0
Trypsin Inhibitor, Bowman-Birk Soybean
0
Trypsin
EC 3.4.21.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
79-86Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.