Solution Structure of the Squash Trypsin Inhibitor MCoTI-II. A New Family for Cyclic Knottins†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (27) ◽  
pp. 7973-7983 ◽  
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
T. Trân Châu Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

Solution Structure of the Macrocyclic Squash Trypsin Inhibitor MCoTI-II, the First Member of a New Family of Cyclic Knottins

2001 ◽  
pp. 387-388
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
Châu T. T. Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides

2012 ◽  
Vol 446 (2) ◽  
pp. 331-331
Author(s):  
P. B. Oparin ◽  
K. S. Mineev ◽  
Y. E. Dunaevsky ◽  
A. S. Arseniev ◽  
M. A. Belozersky ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Plant Defence ◽  
Hairpin Structure ◽  
New Family ◽  
Helical Hairpin

scholarly journals The solution structure of bovine pancreatic trypsin inhibitor at high pressure

2003 ◽  
Vol 12 (9) ◽  
pp. 1971-1979 ◽  
Author(s):  
Michael P. Williamson ◽  
Kazuyuki Akasaka ◽  
Mohamed Refaee
Keyword(s):  
High Pressure ◽  
Trypsin Inhibitor ◽  
Solution Structure ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

scholarly journals Enzymatic Cyclization of a Potent Bowman-Birk Protease Inhibitor, Sunflower Trypsin Inhibitor-1, and Solution Structure of an Acyclic Precursor Peptide

2003 ◽  
Vol 278 (24) ◽  
pp. 21782-21789 ◽  
Author(s):  
Ute C. Marx ◽  
Michael L. J. Korsinczky ◽  
Horst Joachim Schirra ◽  
Alun Jones ◽  
Barrie Condie ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Trypsin Inhibitor ◽  
Solution Structure ◽  
Precursor Peptide ◽  
Acyclic Precursor

The Solution Structure of Antigen MPT64 from Mycobacterium tuberculosis Defines a New Family of Beta-Grasp Proteins

2007 ◽  
Vol 366 (2) ◽  
pp. 375-381 ◽  
Author(s):  
Zhonghua Wang ◽  
Belinda M. Potter ◽  
Amanda M. Gray ◽  
Katherine A. Sacksteder ◽  
Brian V. Geisbrecht ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Solution Structure ◽  
New Family

Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides

2012 ◽  
Vol 446 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Peter B. Oparin ◽  
Konstantin S. Mineev ◽  
Yakov E. Dunaevsky ◽  
Alexander S. Arseniev ◽  
Mikhail A. Belozersky ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Disulfide Bonds ◽  
Plant Defence ◽  
Three Dimensional ◽  
Structural Similarity ◽  
Reversed Phase ◽  
Dimensional Structure ◽  
Amino Acid Residues ◽  
New Family ◽  
Helical Hairpin

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 Arg19. The inhibition constant was determined for BWI-2c against trypsin (1.7×10−10 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.

Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination

2002 ◽  
Vol 58 (9) ◽  
pp. 1448-1461 ◽  
Author(s):  
Ram Thaimattam ◽  
Ewa Tykarska ◽  
Andrzej Bierzynski ◽  
George M. Sheldrick ◽  
Mariusz Jaskolski
Keyword(s):  
Trypsin Inhibitor ◽  
Atomic Resolution ◽  
Metal Coordination ◽  
Squash Trypsin Inhibitor ◽  
Resolution Structure

A New Family of β-Hairpin Mimetics Based on a Trypsin Inhibitor from Sunflower Seeds

ChemBioChem ◽  
2002 ◽  
Vol 3 (4) ◽  
pp. 318-323 ◽  
Author(s):  
Anne Descours ◽  
Kerstin Moehle ◽  
Annabelle Renard ◽  
John A. Robinson
Keyword(s):  
Trypsin Inhibitor ◽  
Sunflower Seeds ◽  
New Family
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