The role of ecotin dimerization in protease inhibition

Eggers, Christopher T.; Wang, Stephanie X.; Fletterick, Robert J.; Craik, Charles S.

doi:10.1006/jmbi.2001.4754

Cited by 41 publications

(45 citation statements)

References 69 publications

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“…These results are consistent with the literature regarding the mutation of the primary site where inhibition that occurs with ecotin-RR (Met84Arg and Met85Arg) improves its interactions with thrombin and a thrombin-like catalytic site using an in silico study and some in vitro enzymatic experiments [21]. It is important to emphasize that the IC 50 provide an apparent inhibition constant under the conditions described and these identical conditions were used for all inhibition studies, making them relative to one another and valid comparisons [37].…”

Section: Discussionsupporting

confidence: 83%

Ecotin: Exploring a feasible antithrombotic profile

Wermelinger

Frattani

Carneiro-Lobo

et al. 2015

International Journal of Biological Macromolecules

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Section: Discussionsupporting

confidence: 83%

Ecotin: Exploring a feasible antithrombotic profile

Wermelinger

Frattani

Carneiro-Lobo

et al. 2015

International Journal of Biological Macromolecules

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“…In this way, the exosite actually makes the inhibitor less specific, or more capable of inhibiting a broad range of proteases, and allows one bacterial inhibitor to protect against a number of host proteases. [13] …”

Section: Competitive Inhibition With Exosite Bindingmentioning

confidence: 99%

Mechanisms of Macromolecular Protease Inhibitors

2010

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“…A homodimeric inhibitor from Escherichia coli, called ecotin, although built of a single domain is active as a dimer in which both monomers provide the proteasebinding surface ( fig. 3) [79]. A comparison of the inhibitory properties of dimeric ecotin with that of an engineered monomeric form reveals a complex and non-additive interplay of binding energies provided by the binding sites located on the two subunits [80].…”

Section: Domain Architecturementioning

confidence: 99%

Canonical protein inhibitors of serine proteases

Krowarsch

Cierpicki

Jeleń

et al. 2003

CMLS, Cell. Mol. Life Sci.

208

189

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Serine proteases and their natural protein inhibitors are among the most intensively studied protein complexes. About 20 structurally diverse inhibitor families have been identified, comprising alpha-helical, beta sheet, and alpha/beta proteins, and different folds of small disulfide-rich proteins. Three different types of inhibitors can be distinguished based on their mechanism of action: canonical (standard mechanism) and non-canonical inhibitors, and serpins. The canonical inhibitors bind to the enzyme through an exposed convex binding loop, which is complementary to the active site of the enzyme. The mechanism of inhibition in this group is always very similar and resembles that of an ideal substrate. The non-canonical inhibitors interact through their N-terminal segment. There are also extensive secondary interactions outside the active site, contributing significantly to the strength, speed, and specificity of recognition. Serpins, similarly to the canonical inhibitors, interact with their target proteases in a substrate-like manner; however, cleavage of a single peptide bond in the binding loop leads to dramatic structural changes.

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The role of ecotin dimerization in protease inhibition

Cited by 41 publications

References 69 publications

Ecotin: Exploring a feasible antithrombotic profile

Ecotin: Exploring a feasible antithrombotic profile

Mechanisms of Macromolecular Protease Inhibitors

Canonical protein inhibitors of serine proteases

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