Mutational analysis of the putative PLA2-inhibiting sequence of annexin 1.
Annexin 1 has been proposed to inhibit phospholipase A2 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 involve in the inhibition of phospholipase A2.
Travé
G
G
Inserm U65, Département Biologie-Santé, Université de Montpellier II, France.
Lees
D
D
Liautard
J P
JP
Widada
J S
JS
D000595:Amino Acid Sequence; D017302:Annexins; D001483:Base Sequence; D002135:Calcium-Binding Proteins / Q000235:genetics* / Q000494:pharmacology; D002460:Cell Line; D004252:DNA Mutational Analysis; D006801:Humans; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D015202:Protein Engineering
D017302:Annexins; D002135:Calcium-Binding Proteins; D010741:Phospholipases A; D054467:Phospholipases A2