| Autor: |
Turkenburg, Johan P., Lamers, Marieke B. A. C., Brzozowski, A. Marek, Wright, Lisa M., Hubbard, Roderick E., Sturt, Simone L., Williams, David H. |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Mar2002, Vol. 58 Issue 3, p451-455, 5p |
| Abstrakt: |
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 Å 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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