Differential structural characteristics, physicochemical properties, and calcium-binding capabilities of annexin A2 wild-type versus E53A, E96A, D162A, E247A and D322A mutants.

Abstract excerpt

Annexin A2 (ANXA2) is a Ca2+-dependent multifunctional protein containing five Ca2+-binding domains, but their functional significance and difference remain unclear. Herein, glutamic acid (E) or aspartic acid (D) in five Ca2+-binding domains of canine ANXA2 (98.82 % and 96.76-99.41 % identical to ANXA2 from human and other mammals, respectively) was substituted by alanine (A) using site-directed mutagenesis....

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