Mad1 (6-21) is the 6-21 fragment of Mad1 protein. Mad1 (6-21) binds to mammalian Sin3A PAH2 with a K_d of ~29 nM.

The PAH2 domain of mSin3A adopts a left-handed, up-and-down, four-helix bundle structure with residues in all four helices as well as in the turn regions defining a compact structural domain with an extensive hydrophobic core. Helices α1 and α2 form a deep hydrophobic pocket, which constitutes the primary interaction surface for the Mad1 (6-21) peptide. The Mad1 (6-21) forms an amphipathic α helix in the complex and interacts with PAH2 mainly through the apolar surface of the helix.

西域 has not independently confirmed the accuracy of these methods. They are for reference only.

• . K Brubaker, et al. Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Cell. 2000 Nov 10;103(4):655-65.  [Content Brief]