Isolation of two cDNA sequences which encode cytotoxic cell proteases.
Two cDNAs which cross-hybridized with cytotoxic cell protease genes were identified in a library generated from a cytotoxic T cell line. Sequence analysis revealed that the two new members of the family contained the three catalytic triad residues which characterize the active sites of serine proteases. A comparison of the protein sequences revealed not only a high degree of homology but also the conservation of some unusual structural features. These include the lack of a disulphide bond which spans the active site serine, the presence of a signal sequence and the inference of a dipeptide activation sequence.
Bleackley
R C
RC
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Duggan
B
B
Ehrman
N
N
Lobe
C G
CG
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics / Q000302:isolation & purification*; D010450:Endopeptidases; D006031:Glycosylation; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000235:genetics*; D013602:T-Lymphocytes, Cytotoxic / Q000201:enzymology*
D008565:Membrane Proteins; D004247:DNA; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase