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Titolo:
High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds
Autore:
Luckett, S; Garcia, RS; Barker, JJ; Konarev, AV; Shewry, PR; Clarke, AR; Brady, RL;
Indirizzi:
Univ Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD Bristol BS8 1TD, Avon, England Univ Oviedo, Dept Analyt Chem, E-33006 Oviedo, Asturias, Spain Univ Oviedo Oviedo Asturias Spain E-33006 E-33006 Oviedo, Asturias, Spain All Russian Inst Plant Protect, St Petersburg, Russia All Russian Inst Plant Protect St Petersburg Russia Petersburg, Russia Univ Bristol, Long Ashton Res Stn, IACR, Dept Agr Sci, Bristol BS41 9AF, Avon, England Univ Bristol Bristol Avon England BS41 9AF ristol BS41 9AF, Avon, England
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 290, anno: 1999,
pagine: 525 - 533
SICI:
0022-2836(19990709)290:2<525:HSOAPC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE BETA-TRYPSIN; BOWMAN-BIRK INHIBITOR; REACTIVE-SITE LOOP; PROTEASE INHIBITORS; CRYSTAL-STRUCTURE; COMPLEXES; REFINEMENT; PATHOGENS; GEOMETRY; DENSITY;
Keywords:
Bowman-Birk inhibitor; trypsin inhibitor; cyclic peptide; sunflower seeds; X-ray crystallography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Brady, RL Univ Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD S8 1TD, Avon, England
Citazione:
S. Luckett et al., "High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds", J MOL BIOL, 290(2), 1999, pp. 525-533

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 (K-i = 100 pM). The crystal structure of this peptide in complex with bovine P-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 highpotency 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 minimalunit required for effective peptide inhibitors of serine proteinases, and will assist in the further design of inhibitors to this widespread class ofenzymes. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:58:21