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![[Figure 2]](kw5112fig2mag.jpg)
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Figure 2
Structure of the Expansion Nα-MH2 domain and its comparison with the human Smad2 (huSmad2) and Smad4 (huSmad4) MH2 domains. (a) Refined structure of the Expansion Nα-MH2 domain including residues 27–236. The structure is displayed as a cartoon representation. Elements of secondary structure are labelled according to the Smad canonical MH2 fold, despite differences in the secondary-structure content in the N-terminus (the Nα helix present in Expansion) and in the region of α2 and β8+9. (b) Superposition of the huSmad2 MH2 domain (PDB entry 1mjs; grey), the human Smad4 MH2 domain (PDB entry 1dd1; orange) and the refined structure of the Nα-MH2 domain of Expansion (PDB entry 4r9p; blue). This view is rotated by 90° with respect to (a). (c) Close-up view of the Nα helix of the Expansion Nα-MH2 domain. The Nα helix (depicted in salmon) and the side chains that contribute to its packing are represented as sticks and labelled. (d) Cartoon and electrostatic potential surface distribution of the Expansion Nα-MH2 domain. (e) Same as in (d) for the huSmad2 MH2 domain (PDB entry 1khx). The L3 region required for phosphorylation recognition is highlighted. (f) The Cα trace of the Nα-MH2 domain and electron-density maps at contour levels of 1σ (0.3186 e Å−3) and 2σ (0.6372 e Å−3). All figures were prepared using PyMOL (Schrödinger). |
![[Figure 2]](kw5112fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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