Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 321446
Title Structural characterization of thyroglobulin type-1 domains of equistatin
Author(s) Galesa, K.; Pain, R.; Jongsma, M.A.; Turk, V.; Lenarci, B.
Source FEBS Letters 539 (2003). - ISSN 0014-5793 - p. 120 - 124.
Department(s) PRI Bioscience
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) human cathepsin-d - cysteine proteinases - pichia-pastoris - actinia-equina - secondary structure - circular-dichroism - protease inhibitor - expression - purification - stability
Abstract Equistatin is a protein composed of three thyroglobulin type-1 domains. It inhibits papain-like cysteine proteinases and the aspartic proteinase, cathepsin D. To determine the structural basis for this inhibition we cloned and expressed the separated domains (eq d-1, eq d-2, eq d-3) in Pichia pastoris. Kinetic constants for the interaction of eq d-1 with papain and that of eq d-2 with cathepsin D are of similar order (subnanomolar) and are comparable to the constants obtained for full-length equistatin. The target proteinase for the third domain remains unknown. Thus, we demonstrate here that thyroglobulin type-1 motifs per se are able to support specific structural features that enable them to inhibit proteases from different classes. The overall conformation of three domains in equistatin is such that the interaction of domains 1 or 2 with their respective target enzymes is not hindered sterically by either domain. In addition, we show that the interaction of eq d-2 with cathepsin D results in conformational changes, which is not the case for the eq d-1/papain interaction
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