SerpinB5, also known as maspin, is considered a tumor suppressor serpin that does not present itself as a protein inhibitor like others of its own family, the serine protease inhibitor superfamily (serpins). Maspin was first identified in 1994 on mammary tissue and breast cancer cell lines (1), but it is also known to be expressed on a wide range of cell types and tissues, mainly in epithelial cells, i. e. in prostate, lung, skin, and corneal stromal cells (2). It differs from ordinary serpins once it does not undergo the stressed (S) to relaxed (R) conformation which is a striking feature of other proteins in serpin’s superfamily. Instead, its G-helix has quite a flexibility, capable of changing the conformation of the protein itself.
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Function
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Structural highlights
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