1y2y
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(New page: 200px<br /><applet load="1y2y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y2y" /> '''Structural Characterization of Nop10p using ...)
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Revision as of 04:24, 21 November 2007
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Structural Characterization of Nop10p using Nuclear Magnetic Resonance Spectroscopy
Overview
The H/ACA small nucleolar ribonucleoprotein (snoRNP) complexes guide the, modification of uridine to pseudouridine at conserved sites in rRNA. The, H/ACA snoRNPs each comprise a target-site-specific snoRNA and four core, proteins, Nop10p, Nhp2p, Gar1p, and the pseudouridine synthase, Cbf5p, in, yeast. The secondary structure of the H/ACA snoRNAs includes two hairpins, that each contain a large internal loop (the pseudouridylation pocket), one or both of which are partially complementary to the target RNA(s). We, have determined the solution structure of an RNA hairpin derived from the, human U65 box H/ACA snoRNA including the pseudouridylation pocket and, adjacent stems, providing the first three-dimensional structural, information on these H/ACA snoRNAs. We have also determined the structure, of Nop10p and investigated its interaction with RNA using NMR, spectroscopy. Nop10p contains a structurally well-defined N-terminal, region composed of a beta-hairpin, and the rest of the protein lacks a, globular structure. Chemical shift mapping of the interaction of RNA, constructs of U65 box H/ACA 3' hairpin with Nop10p shows that the, beta-hairpin binds weakly but specifically to RNA. The unstructured region, of Nop10p likely interacts with Cbf5p.
About this Structure
1Y2Y is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA., Khanna M, Wu H, Johansson C, Caizergues-Ferrer M, Feigon J, RNA. 2006 Jan;12(1):40-52. PMID:16373493
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