1GLO
Crystal Structure of Cys25Ser mutant of human cathepsin S
Summary for 1GLO
| Entry DOI | 10.2210/pdb1glo/pdb |
| Related | 1BXF |
| Descriptor | CATHEPSIN S (2 entities in total) |
| Functional Keywords | cathepsin s, proteinase, inhibitor, hydrolase, thiol proteas |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 23975.90 |
| Authors | Turkenburg, J.P.,Lamers, M.B.A.C.,Brzozowski, A.M.,Wright, L.M.,Hubbard, R.E.,Sturt, S.L.,Williams, D.H. (deposition date: 2001-08-31, release date: 2002-08-29, Last modification date: 2024-11-06) |
| Primary citation | 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 Cited by 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: 11856830DOI: 10.1107/S0907444901021825 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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