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. Author manuscript; available in PMC: 2009 Oct 13.
Published in final edited form as: Curr Proteomics. 2008 Jul 1;5(2):129–137. doi: 10.2174/157016408784911936

Figure 4.

Figure 4

Schematic representation of a Heterotrimeric complex of the core Box H/ACA proteins and complete Box H/ACA RNP. (A) aGar1p, aCbf5p, and aNop10p are capable of forming a trimer in the absence of both a Box H/ACA RNA and Nhp2p. aGar1p interacts with aCbf5p opposite the side of Nop10p (see Rashid et al. 2006 for detail). (B) A schematic composite of the two structures provided by Li and Ye (2006) and Liang et al. (2007). The complete Box H/ACA RNP consists of the four core proteins, a Box H/ACA RNA, and substrate RNA. Nhp2p, Nop10p and the PUA domain of Cbf5p, are responsible for anchoring Cbf5p to the Box H/ACA RNA, and positioning Cbf5p’s catalytic core over the target uridine. (see Li and Ye 2006, and Liang et al. 2007 for atomic structures).