By Philippe Taupin
This publication goals at providing an summary of the present wisdom of cystatins and molecles of the cystatin superfamily, their constitution, physio-and pathological functionality in addition to the course that examine is at the moment aiming for in constructing healing remedies in line with cysteine proteinases and similar molecules. Its objective is to offer the reader a device that serves as a reference within the box of protease inhibitor, their physio-and pathological capabilities and healing strength. It additionally goals at making obtainable to a broader viewers, that doesn't have quick access to clinical courses, a resource of information and data. To acheive this aim, the publication goals at masking largely, systematically, concisely, and extensive, the multifacets of the function of cystatins and molecules of the cystatin superfamily in physiopathology, and emphasize on their healing potentials. Figures, self-explantory schemas and diagrams give a contribution to clarifying and help the knowledge provided.
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Extra info for The Cystatin Superfamily of Proteinase Inhibitors
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Three-dimensional domain swapping is a process for forming dimeric, oligomeric and multimeric proteins. In three-dimensional domain swapping, one domain, a flexible domain, of a multi-domain molecule takes the place of the same domain in another similar molecule. In turn, the flexible domain from the latter molecule takes the same place in another molecule, leading to the formation of multimeric proteins. Multimeric proteins can be either closedended (a) or open-ended (b). One of the requirements for three-dimensional domain swapping is the existence of a flexible domain, capable of unfolding and taking the same place in another similar molecule.
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The Cystatin Superfamily of Proteinase Inhibitors by Philippe Taupin