Structure of a Cys25-->Ser mutant of human cathepsin S.
作者： Johan P. Turkenburg , Marieke B. A. C. Lamers , A. Marek Brzozowski , Lisa M. Wright , Roderick E. Hubbard
DOI: 10.1107/S0907444901021825
关键词:
摘要: Cathepsin S (EC 3.4.22.27), a cysteine proteinase of the papain superfamily, plays critical role in generation major histocompatibility complex (MHC) class II restricted T-cell response by antigen-presenting cells. Therefore, selective inhibition this enzyme may be useful modulating T-cell responses immune-related disorders such as rheumatoid arthritis, multiple sclerosis and extrinsic asthma. The three-dimensional structure at 2.2 A resolution active-site Cys25→Ser mutant presented here an unliganded state provides further insight for design inhibitors.
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