1QTN

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE

Summary for 1QTN

• Entry DOI: 10.2210/pdb1qtn/pdb
• Related PRD ID: PRD_000301
• Descriptor: CASPASE-8, ACETYL-ILE-GLU-THR-ASP-ALDEHYDE, DITHIANE DIOL, ... (5 entities in total)
• Functional Keywords: apoptosis, dithiane-diol, caspase, cysteine-protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q14790 Q14790
• Total number of polymer chains: 3
• Total formula weight: 30334.49

Authors

Watt, W.,Watenpaugh, K.D. (deposition date: 1999-06-28, release date: 2000-09-20, Last modification date: 2023-11-15)

Primary citation

Watt, W.,Koeplinger, K.A.,Mildner, A.M.,Heinrikson, R.L.,Tomasselli, A.G.,Watenpaugh, K.D.
The atomic-resolution structure of human caspase-8, a key activator of apoptosis.
Structure Fold.Des., 7:1135-1143, 1999

PubMed Abstract: Caspases are a family of cysteine proteases that have important intracellular roles in inflammation and apoptosis. Caspase-8 activates downstream caspases which are unable to carry out autocatalytic processing and activation. Caspase-8 is designated as an initiator caspase and is believed to sit at the apex of the Fas- or TNF-mediated apoptotic cascade. In view of this role, the enzyme is an attractive target for the design of inhibitors aimed at blocking the undesirable cell death associated with a range of degenerative disorders.

PubMed: 10508785
DOI: 10.1016/S0969-2126(99)80180-4

Experimental method

X-RAY DIFFRACTION (1.2 Å)