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Ribose zippers

A landmark achievement in RNA structure determination was the solution of the crystal structure of the 160 nucleotide long P4-P6 domain of the Tetrahyme-na group I intron [19,34,35,39]. The P4-P6-domain folds into a compact structure with a sharp turn that is stabilized by tight packing of the heHces. This newly discovered structural element was designated as the ribose-zipper because of the hydrogen bonds between ribose residues of the helices that participate in the structure. In addition, stabiHzation of RNA folds in P4-P6 occurs mainly via... [Pg.104]

Klostermeier, D., and Millar, D. P. (2001). Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms Different energetic contributions from a ribose zipper motif. Biochemistry 40, 11211—11218. [Pg.184]

Ribose zippers Ribose zippers are stabilized by a hydrogen bond network that is formed between two antiparallel strands of RNA that come into close proximity bnt are not base paired. In this network, the hydrogens of the 2 OH s of the 5 nncleotides in both strands interact with the oxygens of the 2 OH s of the 3 nncleotides on the other strand. Hydrogen bonds also form between the 2 OH of the 3 nncleotide on both strands and acceptor groups of the bases at the 5 nucleotides of the other strand. The backbone conformation of a ribose zipper has twofold symmetry. [Pg.89]


See other pages where Ribose zippers is mentioned: [Pg.1638]    [Pg.496]    [Pg.6]    [Pg.1638]    [Pg.496]    [Pg.6]    [Pg.112]    [Pg.190]   
See also in sourсe #XX -- [ Pg.6 ]




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