Abstract
A cDNA clone corresponding to the complete amino acid sequence of a putative protease CCP2 of murine cytotoxic T lymphocytes was isolated and sequenced. The clone encodes a 248-residue long serine esterase. The deduced N-terminal amino acid sequence is identical over 40 residues to that of granzyme C, a protease of unknown function present in granules of cytotoxic lymphocytes. Analysis of the sequence of granzyme C/CCP2 reveals high homology to other granzyme proteases, i.e. granzyme A (40%) and granzyme B (67%) and to rat mast cell protease II (46%). The amino acids lining the specificity pocket are well conserved between granzyme B, C and rat mast cell protease II, but not granzyme A, suggesting a similar general specificity of these three proteases.
Original language | English (US) |
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Pages (from-to) | 318-323 |
Number of pages | 6 |
Journal | Journal of Immunology |
Volume | 140 |
Issue number | 1 |
State | Published - Jan 1 1988 |
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology