Mapping the interfacial binding surface of human secretory group IIa phospholipase A2.

@article{Snitko1997MappingTI,
  title={Mapping the interfacial binding surface of human secretory group IIa phospholipase A2.},
  author={Y Snitko and Rao S Koduri and S K Han and Roohaida Othman and Sharon F Baker and Barbara J. Molini and David Wilton and Michael H Gelb and Wonhwa Cho},
  journal={Biochemistry},
  year={1997},
  volume={36 47},
  pages={14325-33}
}
Human secretory group IIa phospholipase A2 (hIIa-PLA2) contains a large number of prominent cationic patches on its molecular surface and has exceptionally high affinity for anionic surfaces, including anionic membranes. To identify the cationic amino acid residues that support binding of hIIa-PLA2 to anionic membranes, we have performed extensive site-directed mutagenesis of this protein and measured vesicle binding and interfacial kinetic properties of the mutants using polymerized liposomes… CONTINUE READING

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