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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FMR1_HUMAN FMR1_HUMAN]] Translation repressor. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression (By similarity). RNA-binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C). | [[http://www.uniprot.org/uniprot/FMR1_HUMAN FMR1_HUMAN]] Translation repressor. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression (By similarity). RNA-binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fragile X syndrome, a common cause of intellectual disability and autism, is due to mutational silencing of the FMR1 gene leading to the absence of its gene product, FMRP. FMRP is a selective RNA-binding protein owing to two central KH domains and a C-terminal RGG box. However, several properties of the FMRP amino terminus are unresolved. It has been documented for over a decade that the amino terminus has the ability to bind RNA despite having no recognizable functional motifs. Moreover, the amino terminus has recently been shown to bind chromatin and influence the DNA damage response as well as function in the presynaptic space, modulating action potential duration. We report here the amino terminal crystal structures of wild-type FMRP, and a mutant (R138Q) that disrupts the amino terminus function, containing an integral tandem Agenet and discover a novel KH motif. | ||
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| + | Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain.,Myrick LK, Hashimoto H, Cheng X, Warren ST Hum Mol Genet. 2014 Nov 20. pii: ddu586. PMID:25416280<ref>PMID:25416280</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:23, 10 December 2014
FMRP N-terminal domain
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Categories: Cheng, X | Hashimoto, H | Myrick, L K | Warren, S T | Fmr1 | Fmrp | Histone binding | Kh | Nuclear | Rna binding | Tandem agenet | Translation
