Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Huazhong Normal University, Wuhan 430079, People's Republic of China.
Biochem Biophys Res Commun. 2011 Sep 2;412(3):425-8. doi: 10.1016/j.bbrc.2011.07.091. Epub 2011 Jul 28.
Methyl-CpG (mCpG) binding domain protein 4 (MBD4) is a member of mammalian DNA glycosylase superfamily. It contains an amino-proximal methyl-CpG binding domain (MBD) and a C-terminal mismatch-specific glycosylase domain, which is an important molecule believed to be involved in maintaining of genome stability. Herein, we determined the crystal structure of C-terminal glycosylase domain of human MBD4. And the structural alignments of other helix-hairpin-helix (HhH) DNA glycosylases show that the human MBD4 glycosylase domain has the similar active site and the catalytic mechanisms as others. But the different residues in the N-terminal of domain result in the change of charge distribution on the surface of the protein, which suggest the different roles that may relate some diseases.
甲基化CpG 结合域蛋白 4（MBD4）是哺乳动物 DNA 糖苷酶超家族的成员。它包含一个氨基近端甲基化 CpG 结合域（MBD）和一个 C 末端错配特异性糖苷酶域，这是一种被认为参与维持基因组稳定性的重要分子。在此，我们确定了人 MBD4 的 C 末端糖苷酶域的晶体结构。并且其他螺旋-发夹-螺旋（HhH）DNA 糖苷酶的结构比对表明，人 MBD4 糖苷酶域具有与其他酶相似的活性位点和催化机制。但是，结构域 N 端的不同残基导致蛋白质表面电荷分布的变化，这表明可能与某些疾病相关的不同作用。
