User:Daniel Key Takemoto/Sandbox 1: Difference between revisions

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==RGG motif==
==RGG motif==


An important motif of the FMRP is the <scene name='96/969643/Rgg_box/1'>RGG box</scene>, which the protein uses to bind to guanine G-quadruplexes, a structure that consists of nucleic acid folding in which four guanines arrange in a planar conformation stabilized by Hoogsteen-trype hydrogen bonds, named tetrad, and they are stabilized by a K+ cation (green ball in the image). The RNA being represented is the ''sc1'' RNA, and the interaction between them was visualized through NMR. There are <scene name='96/969643/Sc1_gquadruplexes/1'>three G-Quadruplexes</scene> in the ''sc1'' RNA. FMRP RGG motifs seem to prefer binding to specific structures.
An important motif of the FMRP is the <scene name='96/969643/Rgg_box/1'>RGG box</scene>, which the protein uses to bind to guanine G-quadruplexes, a structure that consists of nucleic acid folding in which four guanines arrange in a planar conformation stabilized by Hoogsteen-type hydrogen bonds, named tetrad, and they are stabilized by a K+ cation (green ball in the image). The RNA being represented is the ''sc1'' RNA, and the interaction between them was visualized through NMR. There are <scene name='96/969643/Sc1_gquadruplexes/1'>three G-Quadruplexes</scene> in the ''sc1'' RNA. FMRP RGG motifs seem to prefer binding to specific structures.


Different domains and motifs mediate the RNA binding mechanism, and the exon 15-encoded <scene name='96/969643/Rgg_motif/2'>RGG motif</scene> (arginine - glycine - glycine) and the binding of FMRP to G-rich RNAs in vitro requires only the RGG motif, which occurs through the binding of a '''hydrogen bond between an RNA base and a aminoacid residue'''. The FMRP RGG motif is located in the C-terminal region of the protein and is well conserved in vertebrates. Crystal structure of the complex between the human FMRP RGG motif and G-quadruplex RNA The RGG motif binds to G-quadruplexes when it adopts a sharp turn and specifically binds to guanines from two consecutive G-C base pairs in the duplex-quadruplex junction. Several tetrads can stack in a single G-quadruplex structure and be stabilized further by potassium cations, in the case of FMRP targets, whereas they are destabilized by lithium cations.
Different domains and motifs mediate the RNA binding mechanism, and the exon 15-encoded <scene name='96/969643/Rgg_motif/2'>RGG motif</scene> (arginine - glycine - glycine) and the binding of FMRP to G-rich RNAs in vitro requires only the RGG motif, which occurs through the binding of a '''hydrogen bond between an RNA base and a aminoacid residue'''. The FMRP RGG motif is located in the C-terminal region of the protein and is well conserved in vertebrates. Crystal structure of the complex between the human FMRP RGG motif and G-quadruplex RNA The RGG motif binds to G-quadruplexes when it adopts a sharp turn and specifically binds to guanines from two consecutive G-C base pairs in the duplex-quadruplex junction. Several tetrads can stack in a single G-quadruplex structure and be stabilized further by potassium cations, in the case of FMRP targets, whereas they are destabilized by lithium cations.