STAFF PRIORITY TIME SOLUTION SCATTERING STUDIES ON ANNEXIN XII ASSEMBLY

我们研究了膜联蛋白XII的三种定点突变体（E105 K， E105 K/K68 A、E105 K/K68 A/E76 A），旨在研究 参与分子间相互作用的氨基酸残基 其在Ca 2+诱导的六聚体形成中起重要作用。 我们观察到E105 K的回转半径明显较小， 与野生型相比，存在饱和量的Ca 2 + 在相同的溶液条件下。 六聚体的形成是 如预期的，对于双突变体和三突变体， 从晶体结构上。 因此，我们得出结论，这些氨基酸 残基在Ca 2+诱导的寡聚体形成中至关重要。

We studied three site-directed mutants of annexin XII (E105K, E105K/K68A, E105K/K68A/E76A), aimed at investigating the roles of amino acid residues participating in the intermolecular interaction which plays an important role in the Ca2+-induced hexamer formation. We observed significantly smaller radii of gyration with E105K in the presence of saturated amounts of Ca2+ as compared to the wild type protein in an identical solution condition. The hexamer formation is significantly diminished for the double and triple mutants as expected from the crystal structure. Thus we conclude that these amino acid residues are crucial in the Ca2+-induced oligomer formation.