CRYSTAL STRUCTURES OF HUMAN ANNEXIN A2 IN COMPLEX WITH PHOSPHATIDYL-INOSITOL-4,5

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Annexin A2 is a member of the calcium- and phospholipid binding protein family called annexins. Due to its ability to bind to phospholipid membranes and the cytoskeleton, the protein seems to play a role in membrane-related events such as endocytosis, exocytosis, membrane/membrane and membrane/cytoskeleton linkage. It has been shown recently that annexin A2 specifically associates with parts of the cell membrane containing phosphatidyl-inosiol-4,5-biphosphate. The interaction is specific for phosphatidyl-inositol-4,5-biphosphate and not for other phosphoinositides. The dissociation constant for this complex is in the micromolar range. We have purified recombinant human annexin A2 and crystallized it in the presence of L-alpha-phosphatidylinositol-4,5-diphosphate (the headgroup of the lipid only). We would like to determine the high resolution structure of the protein complex.