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

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)