Recognition of small molecules by a ribonucleopeptide.
In this research, we have design an ATP binding domain that consists of an RNA subunit and a peptide subunit by means of structure-based design approach and in vitro selection method. The RNA subunit is designed to consist of two functional domains; an ATP binding domain with 20 randomized nucleotides and an adjacent stem region that serves as a binding site for the RNA-binding peptide. RNA-peptide receptors to ATP were isolated from a pool of different RNAs by selection with affinity column and enzymatic amplification. Effects of the RNA-binding peptide for the specific ATP binding to the selected RNA-peptide receptors are discussed.
Hagihara
M
M
Institute of Advanced Energy, Kyoto University, Kyoto, Japan.
Morii
T
T
Makino
K
K
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry; D018048:Receptors, Purinergic P2 / Q000737:chemistry; D012261:Ribonucleoproteins / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*
D010455:Peptides; D018048:Receptors, Purinergic P2; D012261:Ribonucleoproteins; D012313:RNA; D000255:Adenosine Triphosphate