1RWW

Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid

Summary for 1RWW

• Entry DOI: 10.2210/pdb1rww/pdb
• Related: 1bmq 1ibc 1ice 1rwk 1rwm 1rwn 1rwo 1rwp 1rwv 1rwx
• Descriptor: Interleukin-1 beta convertase, 4-OXO-3-[(6-{[4-(QUINOXALIN-2-YLAMINO)-BENZOYLAMINO]-METHYL}-PYRIDINE-3-CARBONYL)-AMINO]-BUTYRIC ACID, ... (4 entities in total)
• Functional Keywords: protein-small molecule inhibitor complex, hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P29466 P29466
• Total number of polymer chains: 2
• Total formula weight: 30627.08

Authors

Romanowski, M.J.,Fahr, B.T.,O'Brien, T. (deposition date: 2003-12-17, release date: 2004-12-28, Last modification date: 2024-10-30)

Primary citation

Fahr, B.T.,O'Brien, T.,Pham, P.,Waal, N.D.,Baskaran, S.,Raimundo, B.C.,Lam, J.W.,Sopko, M.M.,Purkey, H.E.,Romanowski, M.J.
Tethering identifies fragment that yields potent inhibitors of human caspase-1.
Bioorg.Med.Chem.Lett., 16:559-562, 2006

PubMed Abstract: Disulfide Tethering was applied to the active site of human caspase-1, resulting in the discovery of a novel, tricyclic molecular fragment that selectively binds in S4. This fragment was developed into a class of potent inhibitors of human caspase-1. Several key analogues determined the optimal distance of the tricycle from the catalytic residues, the relative importance of various features of the tricycle, and the importance of the linker.

PubMed: 16274992
DOI: 10.1016/j.bmcl.2005.10.048

Experimental method

X-RAY DIFFRACTION (2.8 Å)