Analysis of calcium-binding sites in calcium-activated neutral protease.

摘要: Calcium-activated neutral protease (CANP) is a typical intracellular responsible for the processing and turnover of various proteins.1–5 Uncontrolled, CANP can destroy cellular components, leading to disease processes like muscular dystrophy. Hence activity must be tightly regulated. Because absolutely requires calcium activity, plays pivotal role in its regulation. Although many important steps regulation have been clarified, most studies not provided any insight into binding CANP6. Structural analyses revealed existence calmodulin-like domain C-terminal region each two constituent, subunits (80K 30K subunits).7–9 These domains are presumed bind determine sensitivity CANP. Nevertheless, following questions remain unsolved: whether calmodulin indeed calcium; calcium-binding sites exist only domains; and, if so, how ions which EF hand structures functional sites.