More MS news articles for Feb 2002

Structure of a Cys25[right arrow]Ser mutant of human cathepsin S

Acta Crystallogr D Biol Crystallogr 2002 Mar 1;58(Pt 3):451-455
Turkenburg JP, Lamers MB, Brzozowski AM, Wright LM, Hubbard RE, Sturt SL, Williams DH.
York Structural Biology Laboratory, Chemistry Department, University of York, Heslington, York YO10 5DD, England.

Cathepsin S (EC, 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[right arrow]Ser mutant presented here in an unliganded state provides further insight useful for the design of selective enzyme inhibitors.