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Isolation of two cDNA sequences which encode cytotoxic cell proteases
Author(s) -
Bleackley R.Chris,
Duggan Brenda,
Ehrman Nancy,
Lobe Corrinne G.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81323-1
Subject(s) - encode , proteases , complementary dna , cytotoxic t cell , isolation (microbiology) , biology , genetics , computational biology , gene , biochemistry , bioinformatics , enzyme , in vitro
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.