Structural highlights
Function
PRO_MPMV Matrix protein. Nucleocapsid protein p14: Nucleocapsid protein. Capsid protein. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.[PROSITE-ProRule:PRU00275][1] The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.[PROSITE-ProRule:PRU00275][2] Enhances the activity of the reverse transcriptase. May be part of the mature RT.[3]
References
- ↑ Zabransky A, Andreansky M, Hruskova-Heidingsfeldova O, Havlicek V, Hunter E, Ruml T, Pichova I. Three active forms of aspartic proteinase from Mason-Pfizer monkey virus. Virology. 1998 Jun 5;245(2):250-6. PMID:9636364 doi:10.1006/viro.1998.9173
- ↑ Zabransky A, Andreansky M, Hruskova-Heidingsfeldova O, Havlicek V, Hunter E, Ruml T, Pichova I. Three active forms of aspartic proteinase from Mason-Pfizer monkey virus. Virology. 1998 Jun 5;245(2):250-6. PMID:9636364 doi:10.1006/viro.1998.9173
- ↑ Krizova I, Hadravova R, Stokrova J, Gunterova J, Dolezal M, Ruml T, Rumlova M, Pichova I. The G-patch domain of Mason-Pfizer monkey virus is a part of reverse transcriptase. J Virol. 2012 Feb;86(4):1988-98. doi: 10.1128/JVI.06638-11. Epub 2011 Dec 14. PMID:22171253 doi:http://dx.doi.org/10.1128/JVI.06638-11
