Peptide mimics of the Bowman–Birk inhibitor reactive site loop
- 12 January 2002
- journal article
- review article
- Published by Wiley in Peptide Science
- Vol. 66 (2) , 79-92
- https://doi.org/10.1002/bip.10228
Abstract
Bowman–Birk Inhibitors (BBIs) are small highly cross‐linked proteins that typically display an almost symmetrical “double‐headed” structure. Each “head” contains an independent proteinase binding domain. The realization that one BBI molecule could form a 1:1:1 complex with two enzymes led early workers to dissect this activity. Now, after three decades of research, it has been possible to isolate the antiproteinase activity as small (∼11 residues), cyclic, synthetic peptides, which display most of the functional aspects of the protein. More recently, it has been found that these peptide fragments are not just a synthetic curiosity—a natural 14‐residue cyclic peptide (SFTI‐1), which too encapsulates the BBI inhibitory motif, is found to occur in sunflowers. This article reviews the properties of BBI‐based peptides (including SFTI‐1) and discusses the features that are important for inhibitory activity. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 79–92, 2002Keywords
This publication has 61 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Solution structures by 1 H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant 1 1Edited by M. F. SummersJournal of Molecular Biology, 2001
- The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural β-hairpin motifJournal of Molecular Biology, 2001
- RETRACTED: Crystal structure of dengue virus NS3 protease in complex with a bowman-birk inhibitor: implications for flaviviral polyprotein processing and drug designJournal of Molecular Biology, 2000
- Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 å resolution. Structural basis of Janus-faced serine protease inhibitor specificityJournal of Molecular Biology, 2000
- The role of the P2′ position of Bowman-Birk proteinase inhibitor in the inhibition of trypsin: Studies on P2′ variation in cyclic peptides encompassing the reactive site loopBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- The role of threonine in the P 2 position of bowman-birk proteinase inhibitors: studies on P 2 variation in cyclic peptides encompassing the reactive site loop 1 1Edited by A. R. FershtJournal of Molecular Biology, 1998
- Binding of amino acid side-chains to S 1 cavities of serine proteinases 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- Inhibitory properties of nonapeptide loop structures related to reactive sites of soybean Bowman‐Birk inhibitorFEBS Letters, 1978
- Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitorCellular and Molecular Life Sciences, 1975