Document Detail


Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides.
MedLine Citation:
PMID:  22612157     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A new peptide trypsin inhibitor named BWI-2c was obtained from buckwheat (Fagopyrum esculentum) seeds by sequential affinity, ion exchange and reversed-phase chromatography. The peptide was sequenced and found to contain 41 amino acid residues, with four cysteine residues involved in two intramolecular disulfide bonds. Recombinant BWI-2c identical to the natural peptide was produced in Escherichia coli in a form of a cleavable fusion with thioredoxin. The 3D (three-dimensional) structure of the peptide in solution was determined by NMR spectroscopy, revealing two antiparallel α-helices stapled by disulfide bonds. Together with VhTI, a trypsin inhibitor from veronica (Veronica hederifolia), BWI-2c represents a new family of protease inhibitors with an unusual α-helical hairpin fold. The linker sequence between the helices represents the so-called trypsin inhibitory loop responsible for direct binding to the active site of the enzyme that cleaves BWI-2c at the functionally important residue Arg(19). The inhibition constant was determined for BWI-2c against trypsin (1.7×10(-1)0 M), and the peptide was tested on other enzymes, including those from various insect digestive systems, revealing high selectivity to trypsin-like proteases. Structural similarity shared by BWI-2c, VhTI and several other plant defence peptides leads to the acknowledgement of a new widespread family of plant peptides termed α-hairpinins.
Authors:
Peter B Oparin; Konstantin S Mineev; Yakov E Dunaevsky; Alexander S Arseniev; Mikhail A Belozersky; Eugene V Grishin; Tsezi A Egorov; Alexander A Vassilevski
Related Documents :
9485507 - Casp2: report on ab initio predictions.
17239817 - Predicting conotoxin superfamily and family by using pseudo amino acid composition and ...
16622797 - Prediction of standard gibbs energies of the transfer of peptide anions from aqueous so...
8197177 - An algorithm to generate low-resolution protein tertiary structures from knowledge of s...
17576647 - Characterisation of a novel growth hormone variant comprising a thioether link between ...
3781737 - In vitro interactions of opioid peptides with phospholipids. ii. additional spectral ev...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  446     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-07-27     Completed Date:  2012-10-29     Revised Date:  2012-11-02    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  69-77     Citation Subset:  IM    
Affiliation:
M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.
Data Bank Information
Bank Name/Acc. No.:
PDB/2LQX
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Chromatography, Reverse-Phase
Fagopyrum / chemistry*,  physiology
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Peptides / chemistry*,  genetics,  metabolism
Plant Proteins / chemistry*,  genetics,  metabolism
Protein Conformation
Protein Folding
Recombinant Proteins / genetics,  metabolism
Seeds / chemistry
Trypsin Inhibitors / chemistry*,  isolation & purification
Chemical
Reg. No./Substance:
0/Peptides; 0/Plant Proteins; 0/Recombinant Proteins; 0/Trypsin Inhibitors
Comments/Corrections
Erratum In:
Biochem J. 2012 Sep 1;446(2):331

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  MRS in Early and Presymptomatic Carriers of a Novel Octapeptide Repeat Insertion in the Prion Protei...
Next Document:  Myxoid variant of anaplastic large cell lymphoma involving the skin: a case report.