1FI8

RAT GRANZYME B [N66Q] COMPLEXED TO ECOTIN [81-84 IEPD]

Summary for 1FI8

• Entry DOI: 10.2210/pdb1fi8/pdb
• Descriptor: NATURAL KILLER CELL PROTEASE 1, ECOTIN, ... (4 entities in total)
• Functional Keywords: complex (serine protease-inhibitor), protease substrate interactions, beta strand structure, chymotrypsin fold, granzyme b, ecotin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Periplasm: P23827 P23827
• Total number of polymer chains: 6
• Total formula weight: 82799.75

Authors

Waugh, S.M.,Harris, J.L.,Fletterick, R.J.,Craik, C.S. (deposition date: 2000-08-03, release date: 2000-09-13, Last modification date: 2024-10-16)

Primary citation

Waugh, S.M.,Harris, J.L.,Fletterick, R.,Craik, C.S.
The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity
Nat.Struct.Biol., 7:762-765, 2000

PubMed Abstract: Granzyme B is a serine protease of the chymotrypsin fold that mediates cell death by cytotoxic lymphocytes. It is a processing enzyme, requiring extended peptide substrates containing an Asp residue. The determinants that allow for this substrate specificity are revealed in the three-dimensional structure of granzyme B in complex with a macromolecular inhibitor. The primary specificity for Asp occurs through a side-on interaction with Arg 226, a buried Arg side chain of granzyme B. An additional nine amino acids make contact with the substrate and define the granzyme B extended substrate specificity profile. The substrate determinants found in this structure are shared by other members of this protein class and help to reveal the properties that define substrate specificity.

PubMed: 10966646
DOI: 10.1038/78992

Experimental method

X-RAY DIFFRACTION (2.2 Å)