4QVZ

FMRP N-terminal domain

Summary for 4QVZ

• Entry DOI: 10.2210/pdb4qvz/pdb
• Related: 4QW2
• Descriptor: Fragile X mental retardation protein 1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: fmrp, fmr1, tandem agenet, kh, histone binding, rna binding, nuclear, translation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q06787
• Total number of polymer chains: 2
• Total formula weight: 49946.80

Authors

Myrick, L.K.,Hashimoto, H.,Cheng, X.,Warren, S.T. (deposition date: 2014-07-16, release date: 2014-12-03, Last modification date: 2023-09-20)

Primary citation

Myrick, L.K.,Hashimoto, H.,Cheng, X.,Warren, S.T.
Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain.
Hum.Mol.Genet., 24:1733-1740, 2015

PubMed Abstract: 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, fragile X mental retardation protein (FMRP). FMRP is a selective RNA binding protein owing to two central K-homology domains and a C-terminal arginine-glycine-glycine (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.

PubMed: 25416280
DOI: 10.1093/hmg/ddu586

Experimental method

X-RAY DIFFRACTION (3.195 Å)