1GLO

Crystal Structure of Cys25Ser mutant of human cathepsin S

1GLO の概要

• エントリーDOI: 10.2210/pdb1glo/pdb
• 関連するPDBエントリー: 1BXF
• 分子名称: CATHEPSIN S (2 entities in total)
• 機能のキーワード: cathepsin s, proteinase, inhibitor, hydrolase, thiol proteas
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23975.90

構造登録者

Turkenburg, J.P.,Lamers, M.B.A.C.,Brzozowski, A.M.,Wright, L.M.,Hubbard, R.E.,Sturt, S.L.,Williams, D.H. (登録日: 2001-08-31, 公開日: 2002-08-29, 最終更新日: 2024-11-06)

主引用文献

Turkenburg, J.P.,Lamers, M.B.A.C.,Brzozowski, A.M.,Wright, L.M.,Hubbard, R.E.,Sturt, S.L.,Williams, D.H.
Structure of a Cys25->Ser Mutant of Human Cathepsin Cathepsin S
Acta Crystallogr.,Sect.D, 58:451-, 2002

PubMed 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.

PubMed: 11856830
DOI: 10.1107/S0907444901021825

実験手法

X-RAY DIFFRACTION (2.2 Å)