Abstract
The box H/ACA ribonucleoproteins (RNPs) are protein-RNA complexes responsible for pseudouridylation, the most abundant post-transcriptional modification of cellular RNAs. Integrity of its box H/ACA domain is also essential for assembly and stability of the human telomerase RNP. The recent publication of the complete box H/ACA RNP structures combined with the previously reported structures of the protein and RNA components makes it possible to deduce the structural accommodation that accompanies assembly of the full particle. This analysis reveals how the protein components distort the RNA component of the RNP, enabling productive docking of the substrate RNA into the enzymatic active site.