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Allostery in trypsin-like proteases suggests new therapeutic strategies

Paper ID Volume ID Publish Year Pages File Format Full-Text
37067 45305 2011 9 PDF Available
Title
Allostery in trypsin-like proteases suggests new therapeutic strategies
Abstract

Trypsin-like proteases (TLPs) are a large family of enzymes responsible for digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis and immunity. A current paradigm posits that the irreversible transition from an inactive zymogen to the active protease form enables productive interaction with substrate and catalysis. Analysis of the entire structural database reveals two distinct conformations of the active site: one fully accessible to substrate (E) and the other occluded by the collapse of a specific segment (E*). The allosteric E*–E equilibrium provides a reversible mechanism for activity and regulation in addition to the irreversible zymogen to protease conversion and points to new therapeutic strategies aimed at inhibiting or activating the enzyme. In this review, we discuss relevant examples, with emphasis on the rational engineering of anticoagulant thrombin mutants.

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Allostery in trypsin-like proteases suggests new therapeutic strategies
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Publisher
Database: Elsevier - ScienceDirect
Journal: - Volume 29, Issue 11, November 2011, Pages 577–585
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
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Online Support
Any Questions? feel free to contact us