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Structure of a Cys25-->Ser mutant of human cathepsin S
Johan P Turkenburg1, Marieke B A C Lamers, A Marek Brzozowski
1York Structural Biology Laboratory, Chemistry Department, University of York, Heslington, York YO10 5DD, England.
Abstract:
Cathepsin S (EC 3.4.22.27), a cysteine proteinase of the papain superfamily, plays a critical role in the generation of a major histocompatibility complex (MHC) class II restricted T-cell response by antigen-presenting cells. Therefore, selective inhibition of this enzyme may be useful in modulating class II restricted T-cell responses in immune-related disorders such as rheumatoid arthritis, multiple sclerosis and extrinsic asthma. The three-dimensional structure at 2.2 A resolution of the active-site Cys25-->Ser mutant presented here in an unliganded state provides further insight useful for the design of selective enzyme inhibitors.