User:Daniel Key Takemoto/Sandbox 1
From Proteopedia
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==N-terminal domain== | ==N-terminal domain== | ||
| - | <StructureSection load='4QVZ' size=' | + | <StructureSection load='4QVZ' size='240' side='right' caption='Caption for this structure' scene=''> |
==RGG motif== | ==RGG motif== | ||
| - | <StructureSection load='5DE5' size=' | + | <StructureSection load='5DE5' size='240' side='right' caption='Caption for this structure' scene=''> |
Different domains and motifs mediate the RNA binding mechanism and the exon 15-encoded RGG (arginine - glycine - glycine) motif is one of them. The RGG motif is well conserved in vertebrates.To easily represent the RGG motif binding to a RNA, this motif will be highlitghted in the scene <scene name='96/969643/Rgg_motif_binding_to_rna/16'>Crystal structure of the complex between human FMRP RGG motif and G-quadruplex RNA.</scene>. Several tetrads can stack in a single G-quadruplex structure and be stabilized further by potassium cations, in the case of FMRP targets, whereas destabilized by lithium cations. FMRP RGG motifs seem to prefer binding to specific structures, not linear motifs. Therefore, the understanding of the interaction RGG-RNA is important for the comprehension of the FMRP and FXS. | Different domains and motifs mediate the RNA binding mechanism and the exon 15-encoded RGG (arginine - glycine - glycine) motif is one of them. The RGG motif is well conserved in vertebrates.To easily represent the RGG motif binding to a RNA, this motif will be highlitghted in the scene <scene name='96/969643/Rgg_motif_binding_to_rna/16'>Crystal structure of the complex between human FMRP RGG motif and G-quadruplex RNA.</scene>. Several tetrads can stack in a single G-quadruplex structure and be stabilized further by potassium cations, in the case of FMRP targets, whereas destabilized by lithium cations. FMRP RGG motifs seem to prefer binding to specific structures, not linear motifs. Therefore, the understanding of the interaction RGG-RNA is important for the comprehension of the FMRP and FXS. | ||
Revision as of 20:57, 9 June 2023
Structure and functions
Fragile X messenger ribonucleoprotein (FMRP) is encoded by the fragile X messenger ribonucleoprotein 1 (FMR1) gene, located in the X chromossome, associated with the fragile X syndrome (FXS), Fragile X Tremor/Ataxia Syndrome (FXTAS) and Premature Ovarian Failure (POF1). FMRP functions as a synaptic regulator by binding to mRNAs and inhibiting its translation, therefore regulating the synthesis of proteins in the synapse. It is also a RNA binding protein, which is reponsible for the transportation of mRNAs to cytoplam. The FMRP can also bind to its own FMR1 transcripts, possibly a self-regulatory mechanism. The RGG motif bind to G-quadruplexes, secondary structures formed in some RNAs. The structure being represented on the right represents the FMRP RGG motif and the G-quadruplex secondary structure in the RNA. The protein structure was obtained by X-ray diffraction with a 3 Å resolution [1]
