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Mutational analysis of the putative PLA 2 ‐inhibiting sequence of annexin 1
Author(s) -
Travé Gilles,
Lees Delphine,
Liautard Jean-Pierre,
Sri Widada Joannes
Publication year - 1991
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(91)81146-y
Subject(s) - mutant , annexin , phospholipase , biochemistry , peptide sequence , recombinant dna , sequence (biology) , chemistry , phospholipase a , point mutation , biology , phospholipase a2 , microbiology and biotechnology , enzyme , in vitro , gene
Annexin 1 has been proposed to inhibit phospholipase A 2 by direct interaction through a specific amino acid sequence spanning residues 246–254. The possible role of this region was investigated by protein engineering. Three point mutations and a deletion have been performed. The four mutant proteins have been expressed in E. coli , purified and tested for calcium and lipid binding, and for phospholipase inhibition. All mutant proteins conserved the properties of the wild‐type recombinant protein. This result clearly demonstrates that this part of the molecule is not involved in the inhibition of phospholipase A 2 .