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• W2101348082 abstract "α-Type phospholipase A₂ inhibitory protein (PLIα) from the serum of the venomous snake <i>Gloydius brevicaudus, Gb</i>PLIα,isone of the protective endogenous proteins that neutralizes its own venom phospholipase A₂ (PLA₂), and it is a homotrimer of subunits having a C-type lectin-like domain. The nonvenomous snake <i>Elaphe quadrivirgata</i> has a homologous serum protein, <i>Eq</i>PLIα-LP, that does not show any inhibitory activity against various snake venom PLA₂s (Okumura, K., Inoue, S., Ikeda, K., and Hayashi, K. (2003) <i>IUBMB Life</i> 55, 539–545). By constructing <i>Gb</i>PLIα-<i>Eq-</i> PLIα-LP chimeric proteins, we have mapped the residues important in conferring <i>Gb</i>PLIα inhibitory activity on region 13–36 in the primary structure of <i>Gb</i>PLIα. Noninhibitory <i>Eq</i>PLIα-LP showed comparable inhibitory activity only when this region was replaced with that of <i>Gb</i>PLIα. Further, mutational analysis of the candidate residues revealed that the individual <i>Gb</i>PLIα to <i>Eq</i>PLIα-LP residue substitutions N26K, K28E, D29N, and Y144S each produced a mutant <i>Gb</i>PLIα protein with reduced inhibitory activity, with the single N26K substitution having the most significant effect. Residues 13–36 were suspected to be located in the helical neck region of the <i>Gb</i>PLIα trimer. Therefore, the region of <i>Gb</i>PLIα responsible for PLA₂ inhibition was distinct from the carbohydrate-binding site of the homologous C-type lectin." @default.
• W2101348082 created "2016-06-24" @default.
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• W2101348082 date "2005-11-01" @default.
• W2101348082 modified "2023-09-30" @default.
• W2101348082 title "Mapping the Region of the α-Type Phospholipase A2 Inhibitor Responsible for Its Inhibitory Activity" @default.
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• W2101348082 doi "https://doi.org/10.1074/jbc.m507250200" @default.
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