Myeloid and erythroid nuclear termination stage-specific protein explained

Myeloid and erythroid nuclear termination stage-specific protein (MENT) is a member of the serpin family of protease inhibitors, and participates in DNA and chromatin condensation.^[1] Alongside its ability to condense chromatin, MENT is also an effective inhibitor of the proteases cathepsin K, cathepsin L, and cathepsin V, all of which are cysteine proteases.^[2] As such, although MENT is structurally classified as a member of the serpin family, it is functionally termed a "cross-class inhibitor," as it is a cysteine rather than a serine protease inhibitor.

External links

• The MEROPS online database for peptidases and their inhibitors: I04.033

Notes and References

1. McGowan S, Buckle AM, Irving JA, etal . X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation . EMBO J. . 25 . 13 . 3144–55 . July 2006 . 16810322 . 1500978 . 10.1038/sj.emboj.7601201 .
2. Irving JA, Shushanov SS, Pike RN, etal . Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation . J. Biol. Chem. . 277 . 15 . 13192–201 . April 2002 . 11821386 . 10.1074/jbc.M108460200 . free .