Structural highlights
Function
MSRB2_MOUSE Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kim HY, Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell. 2004 Mar;15(3):1055-64. Epub 2003 Dec 29. PMID:14699060 doi:http://dx.doi.org/10.1091/mbc.E03-08-0629
- ↑ Lee BC, Peterfi Z, Hoffmann FW, Moore RE, Kaya A, Avanesov A, Tarrago L, Zhou Y, Weerapana E, Fomenko DE, Hoffmann PR, Gladyshev VN. MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation. Mol Cell. 2013 Aug 8;51(3):397-404. doi: 10.1016/j.molcel.2013.06.019. Epub 2013 , Aug 1. PMID:23911929 doi:http://dx.doi.org/10.1016/j.molcel.2013.06.019
