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The p41 Fragment Story
Author(s) -
Turk Dusan,
Guncar Gregor,
Turk Vito
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/713803477
Subject(s) - proteases , cathepsin , thyroglobulin , cleavage (geology) , cysteine , cathepsin b , papain , biology , cathepsin l , chemistry , microbiology and biotechnology , biochemistry , computational biology , genetics , enzyme , antibody , paleontology , fracture (geology)
Abstract The discovery of a fragment from the p41 form of invariant chain tightly bound to cathepsin L provided the first direct link between MHC class II molecules and the regulation of activity of lysosomal cysteine proteases. We recently determined the crystal structure of this p41 invariant chain fragment in complex with cathepsin L[EMBO J. 18, 793 803 (1999)]. This structure explains the specificity of the observed interactions and actually provides a tool, which can be utilized by means of molecular biology, to explore and understand the specificity of thyroglobulin type I domains and thus allow the design of specific inhibitors of papain‐like cysteine proteases. The structure further supports the hypothesis that the thyroglobulin type I and II domains present in various proteins, sometimes in multiple repeats, are regulatory elements of the processing of these proteins by proteolytic cleavage.