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![[Figure 3]](kw5130fig3mag.jpg)
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Figure 3
Cartoon of the U4 core domain. The re-refined model confirmed the architecture described by Leung et al. (2011  ). The seven Sm proteins form a ring by β4–β5 hydrogen bonding across every subunit interface. The protein order viewed from the flat face (top) of the ring is (clockwise) SmF–SmE–SmG–SmD3–SmB–SmD1–SmD2 (Kambach et al., 1999). The Sm-site nonanucleotides of U4 snRNA are bound inside the central hole flanked by Stem II on the flat face and Stem III on the tapered face. The N-terminus of helix H0 in SmD2 is in contact with the bend in Stem II. The lysine-rich L4 loop of SmD2 makes charge interactions with the phosphate backbone of Stem III. |
![[Figure 3]](kw5130fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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