Acta Crystallographica Section D

Biological Crystallography

Volume 58, Part 3 (March 2002)

research papers

 

Structure of a Cys25Ser mutant of human cathepsin S

J. P. Turkenburg, M. B. A. C. Lamers, A. M. Brzozowski, L. M. Wright, R. E. Hubbard, S. L. Sturt and D. H. Williams

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 Å resolution of the active-site Cys25Ser mutant presented here in an unliganded state provides further insight useful for the design of selective enzyme inhibitors.

PDB reference: 1glo

Keywords: cathepsin S; cysteine proteinase; inhibitor.

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