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Ecotin: lessons on survival in a protease-filled world
M E McGrath1, S A Gillmor, R J Fletterick
1Khepri Pharmaceuticals, Inc., South San Francisco, California 94080, USA.
Protein Science : a Publication of the Protein Society
|February 1, 1995
Summary
Ecotin, an Escherichia coli protein, potently inhibits diverse serine proteases by adapting its flexible structure. This challenges traditional views on enzyme specificity and protein interactions.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Ecotin is a 142-amino acid periplasmic protein from Escherichia coli.
- It is known to inhibit various homologous serine proteases with different substrate specificities.
Purpose of the Study:
- To elucidate the structural and functional basis of ecotin's broad-spectrum serine protease inhibition.
- To investigate the molecular mechanisms underlying ecotin's interaction with serine proteases.
Main Methods:
- Structural studies of ecotin:serine protease complexes.
- Functional assays to assess inhibition efficacy against a panel of serine proteases.
Main Results:
- Ecotin effectively inhibits a wide range of serine proteases, including elastases, chymotrypsin, trypsin, factor Xa, and kallikrein.
- Structural analysis reveals ecotin's flexibility allows it to bind diverse proteases.
- Complex structures demonstrate how ecotin interferes with protease function.
Conclusions:
- Ecotin's remarkable ability to inhibit a large subset of chymotrypsin-family serine proteases is confirmed.
- The findings necessitate a reevaluation of protein-protein interaction specificity.
- Ecotin's adaptable binding mechanism highlights innate flexibility as key to broad inhibitory function.
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