title: Two decades of thyroglobulin type-1 domain research.
abstract: Thyroglobulin type-1 repeats are primarily found in thyroglobulin and several other functionally unrelated proteins. Because a few of them exhibit inhibitory activity against cysteine proteases they were named thyropins (thyroglobulin type-1 domain protease inhibitors). In contrast to cystatins, the best-characterized group of papain-like protease inhibitors, they exhibit greater selectivity in their interactions with target proteases. Interestingly, a few members inhibit aspartic protease cathepsin D and metalloproteases. In contrast to the inhibitory fragment of the major histocompatibility complex class II-associated p41 form of invariant chain, whose structural integrity appears mandatory for its inhibitory properties, short polypeptides derived from insulin-like growth factor-binding proteins exhibit the same activity as the structure of the whole fragment. Taken together, the results indicate that the thyroglobulin type-1 repeat is a structural motif occasionally employed as an inhibitor of proteases.
authors.affiliation: Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, SI-1000, Ljubljana, Slovenia.
authors.forename: Marko
authors.initials: M
authors.lastname: Mihelic
authors.forename: Dusan
authors.initials: D
authors.lastname: Turk
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013954:Thyroglobulin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011480:Protease Inhibitors; D013954:Thyroglobulin