Protein structure analysis ribozyme

In mid-1997 an international conference took place in Santa Cruz, USA, in which, for the first time, the exclusive topic was structural aspects of RNA molecules. A report covering this meeting contains an impressive graphic which shows the RNA structures, RNA/DNA complexes, and RNA/protein complexes contained in the brookhaven database as a function of the year of their publication [29]. Between 1988 and 1993 there were just 20. However, in 1996 alone no less than 41 structures appeared. These new dimensions were headed by the crystal structural elucidation of the first larger RNA molecule since the first crystal structure of tRNA in 1973 [30], the 48 nucleotide long hammerhead ribo-zyme (HHR) [31-33]. This landmark achievement was followed by a crystal structure analysis of the P4-P6-domain of a group I intron [34-36] and, more recently, a crystal structure of the hepatitis delta virus ribozyme [37]. 

Group I introns are ribozymes that carry out self-splicing in vivo. Protein components help to stabilize the folded intron structure as shown by X-ray crystal structure analysis. The protein does not have to be long short peptides are sufficient for stabilization. Moreover, RNA templates are capable of ligating short peptides into longer active molecules. It is essential to realize that even short ones can exhibit a defined secondary structure. 

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